Contents

1. Cell Organells
2. Cell Membranes: Structure and Function
3. Amino Acids: Structure and Properties
4. Proteins: Structure and Function
5. Enzymology-I
6. Enzymology-II: Iso-Enzymes and Clinical Enzymology
7. Methods of Separation & Purification of Biological Compounds, Methods of Study of
Metabolism
8. Carbohydrates-I:Chemistry, Digestion and Absorption
9. Carbohydrates-II: Major Metabolic Pathways of Glucose, Glycolysis,
Gluconeogenesis, Glycogen Metabolism
10. Carbohydrates-III: Regulation of Blood Sugar, Insulin and Diabets Mellitus
11. Carbohydrates-IV: Other Metabolic Pathways (HMP Shunt Pathway, Fructose,
Galactose,
12. Lipids-I: Chemistry, Digestion and Absorption of Lipids
13. Lipids-II: Metabolism of Fatty acids, Fatty acid oxidation, Fatty acid synthesis,
Lipolysis, Ketone bodies
14. Lipids-III: Cholesterol, Lipoproteins and Cardiovascular Diseases
15. Lipids-IV: MCFA, PUFA and Prostaglandins
16. Lipids-V: Compound Lipids
17. Amino Acid Metabolism-I: General: Digestion, Absorption, Transamination, Urea
18. Amino Acid Metabolism-II: Simple, Hydroxy and Sulfur Containing Amino Acids
Glycine, Serine, Alanine, Threonine, Methionine, Cysteine
19. Amino Acid Metabolism-III: Acidic, Basic and Branched Chain Amino Acids,
Glutamic acid, Glutamine, Aspartic acid, Asparagine, Lysine, Nitric Oxide, Valine,
Leucine, Isoleucine
20. Amino Acid Metabolism-IV: Aromatic Amino Acids: Phenyl alanine, Tyrosine,
Tryptophan, Histidine
21. Amino Acid Metabolism-V: Inter-relations of Amino Acid Metabolisms, One Carbon
Metabolism, Amino Acidurias
22. Citric Acid Cycle
23. Electron Transport Chain
24. Free Radicals and Anti-oxidants
25. Plasma Proteins
26. Immunochemistry
27. Specialised Proteins: Collagen, Myosin
28. Heme Synthesis and Breakdown
29. Haemoglobins
30. Vitamin-I: Fat Soluble Vitamins: A, D, E and K
31. Vitamin-II: Water soluble vitamins
32. Mineral Metabolism
33. Energy Metabolism and Nutrition
34. Detoxification and Biotransformation of Xenobiotics
35. Biochemical Aspects of Environmental Pollution
36. Acid Base Balance and pH
37. Electrolyte and Water Balance
38. Molecular Biology-I: Nucleotides, Chemistry and Metabolism
39. Molecular Biology-II: DNA structure and Replication
40. Molecular Biology-III: Transcription and Translation
41. Molecular Biology-IV: Molecular Genetics and Control of Gene Expression
42. Molecular Biology-V: Recombinant DNA Technology and Gene Therapy
43. Biochemistry of AIDS
44. Biochemistry of Cancer
45. Applications of Radio-isotopes in Medicine
46. Body Fluids
47. Hormones-I: Mechanism of Action of Hormones
48. Hormones-II: Pituitary Hormones
49. Hormones-III: Steroid Hormones
50. Hormones-IV: Thyroid Hormones
51. Clinical Biochemistry-I:
52. Clinical Biochemistry-II: Liver and Gastric Function Tests
53. Clinical Biochemistry-III: Kidney Function Tests
Viva.based on Textbook of Biochemistry

Cell Organelles
Q. What is the function of Golgi complex?
A. Maturation and processing of nascent proteins, glycosylation of proteins,
secretion newly synthesised proteins

Q. What is the function of endoplasmic reticulum?

A. Biosynthesis of proteins, drug metabolism, desaturation of fatty acids.

Q. What is the marker enzyme for endoplasmic reticulum?

A. Glucose-6-phosphatase

Q. Where does protein synthesis take place?

A. On the walls of endoplasmic reticulum and also in cytosol

Q. What are cathepsins?

A. They are intracellular proteolytic enzymes

Q. What is the function of lysosomes?

A. They are bags of hydrolytic enzymes that bring about degradation of
macromolecules

Q. What is lysozyme?
A. It is an enzyme present in external secretions

Q. What are peroxisomes?

A. They contain peroxidase and catalase, necessary for destroying the
unwanted free radicals.

Q. What are the important metabolic events taking place in cytoplasm?

A. Glycolysis (Embden-Meyerhof pathway), HMP shunt pathway, glycogen
metabolism, Fatty acid synthesis, Synthesis of nucleotides, Degradation of amino
acids

Q. What is the function of mitochondria?

A. Generation of ATP

Q. What are the important metabolic events taking place in mitochondria?

A. TCA cycle, electron transport chain, beta oxida-tion of fatty acids and urea
cycle
Cell Membranes:Structure and Function
Q. What are ecto-enzymes?
A. They are enzymes seen on the outer part of cell membrane .

Q. Give examples of ecto-enzymes.

A. Alkaline phosphatase, 5.nucleotidase .

Q. How do you describe the structure of cell membrane?

A. Fluid mosaic model .

Q. What are the characteristics of fluid mosaic model?.

A. Membrane is composed of lipid bilayer. Phospho-lipids are arranged in bilayers with
a hydrophobic core.

Q. What do you mean by fluidity of the membrane?

A. The lipid bilayer shows free lateral movement of its components; but flip-flop
movement is restricted .

Q. What are the components of membrane that alter the fluidity?

A. Cholesterol and unsaturated fatty acids .

Q. What are the different types of transport mechanisms?

A. Passive and active. Passive type is subclassified as simple diffusion and facilitated
diffusion.

Q. What are the salient features of facilitated diffusion?

A. It is carrier mediated. It does not require energy directly.

Q. Can you give an example of facilitated transport?

A. Glucose transporters.

Q. What are ion channels?

A. They are special devices for quick transport of electrolytes.

Q. Give some examples of ion channels.

A. Ion channels specific for calcium, potassium and chloride.

Q. What are ionophores?

A. They are transport antibiotics which increase the permeability of membrane to ions,
e.g. valinomycin, gramicidin.

Q. What are the salient features of active transport?

A. It requires transporters. It requires energy. Transport is generally unidirectional.
Q. Give examples of active transport systems.
A. Sodium pump, calcium pump.

Q. What is the importance of sodium pump?

A. Cell has low intracellular sodium; but concentration of potassium inside the cell is
high; this is maintained by sodium pump. About 40% of the total energy expenditure in a
cell is used for this active transport system.

Q. How does sodium pump work?

A. It is called sodium-potassium activated ATPase. Hydrolysis of one molecule of ATP
can result in expulsion of 3 sodium ions and influx of 2 potassium ions.

Q. What is its clinical significance?

A. Digoxin increases the contractility of the cardiac muscle, by inhibiting the sodium
pump.

Q. What is a uniport?
A. It carries single solute across the membrane.

Q. Give examples of uniport.

A. Glucose transporter (GluT2) operating in most of the cells is an example. Calcium
pump is another example.

Q. What is co-transport?
A. If transfer of one molecule depends on simultaneous or sequential transfer of another
molecule, it is called co-transport system.

Q. How are co-transport systems classified?

A. The cotransport system may be symport or antiport.

Q. What is symport?
A. In symport, the transporter carries two solutes in the same direction across the
membrane.

Q. Give examples of symport.

A. Sodium dependent glucose transporter (SgluT) . Phlorhizin, an inhibitor of sodium
dependent cotransport of glucose, especially in the proximal convoluted tubules of
kidney, produces renal damage and results in renal diabetes. Amino acid transport is
another example for symport.

Q. What is antiport system?.

A. The antiport system carries two solutes or ions in opposite direction.

Q. Give examples of antiport.

A. Sodium pump or chloride-bicarbonate exchange in RBC
Q. What is endocytosis?.
A. It is the mechanism by which cells internalise extracellular macromolecules.

Q. What is pinocytosis?.
A. It is receptor mediated. Low Density Lipoprotein(LDL) binds to the LDL receptor and
the complex is later internalised. These vesicles are coated with Clathrin. .

Q. What is phagocytosis.
A. It is the engulfment and internalisation of large particles such as bacteria by
macrophages and granulocytes.

Q. What is respiratory burst.

A. During phagocytosis, there is an increase in oxygen consumption with formation of
the superoxide ion.

Amino Acids: Structure and Properties

Q. How do you classify amino acids?
A. Based on the structure, amino acids are classified into: Simple amino acids,
Branched chain amino acids, Hydroxy amino acids, Sulfur containing amino acids,
Amino acids with amide group, Acidic amino acids, Basic amino acids, Aromatic
amino acids, Heterocyclic amino acids, Imino acid and Derived amino acids.

Q. What are branched chain amino acids?

A. Valine, leucine and isoleucine.

Q. What are hydroxy amino acids?

A. Serine and threonine.

Q. Name the Sulfur containing amino acids.

A. Cysteine and methionine.

Q. Name the acidic amino acids.

A. Aspartic acid and glutamic acid.

Q. What are the basic amino acids?

A. Lysine and arginine.

Q. Which amino acid has a net positive charge at physiological pH?

A. Arginine and lysine.

Q. Amino acid containing a thio-ether bond is.

A. Methionine.
Q. Give examples of amino acids with hydrophobic side chains.
A. Valine, leucine, isoleucine.

Q. Give the names of aromatic amino acids.

A. Phenylalanine and tyrosine.

Q. What are heterocyclic amino acids?

A. Tryptophan and histidine.

Q. Give an example of an imino acid.

A. Proline.

Q. Give examples of derived amino acids.

A. Hydroxy proline, hydroxy lysine, ornithine, citrulline, homocysteine.

Q. Arginine contains which special group?

A. Guanidinium group (-NH-CNH-NH2).

Q. Benzene group is present in which amino acid?

A. Phenyl alanine.

Q. Phenol group is present in which amino acid?

A. Tyrosine.

Q. Tryptophan contains what special group?

A. Indole group.

Q. Which special group is present in Histidine?

A. Imidazole group.

Q. Name some hydrophobic amino acids.

A. Valine, leucine and isoleucine.

Q. Pyrrolidine group is present in which amino acid?

A. Proline.

Q. Hydrophobic bonds are formed in protein between which amino acids?

A. Valine, leucine and isoleucine residues.

Q. What is the basis of classification of amino acids into ketogenic and glucogenic?
A. Ketogenic amino acids enter into the metabolic pathway of fats, while
glucogenic amino acids enter the pathway of glucose metabolism.
Q. Name a purely ketogenic amino acid.
A. Leucine.

Q. Name some glucogenic amino acids.

A. Glycine; serine; aspartic acid.

Q. Which amino acid is synthesised after it gets incorporated into the protein?
A. Hydroxyproline.

Q. What are essential amino acids?

A. They cannot be synthesized in the body; and so, they are to be provided in the diet.

Q. How many amino acids are essential?

A. Eight amino acids are essential; two are semi-essential and the rest 10 are non-
essential.

Q. Are non-essential amino acids necessary for the body?

A. They are also necessary for protein synthesis, but they can be synthesized by the
body and need not be essentially present in the diet .

Q. Name any three essential amino acids.

A. Isoleucine, leucine, threonine.

Q. Is phenyl alanine an essential amino acid?

A. Yes.

Q. What about Tyrosine? A. Tyrosine is non-essential, it is synthesized from

phenyl alanine.

Q. Name the semi-essential amino acids.

A. Histidine and arginine.

Q. Why are they called semi-essential?

A. Because growing children require them in food. But they are not essential for the
adult individual.

Q. What is iso-electric point?.

A. The pH at which the molecule carries no net charge is called iso-electric point.

Q. What are the characteristic features of iso-electric pH.

A. At iso-electric point the amino acid will carry no net charge, there is no mobility in
electrical field, solubility will be minimum, the tendency for precipitation will be maximum
Q. What is the speciality of Histidine?
A. The pK value of Histidine is 6.1, and therefore effective as a buffer at the
physiological pH of 7.4. The buffering capacity of plasma proteins and hemoglobin is
mainly due to histidine residue.

Q. Which is the amino acid having maximum buffering capacity at physiological pH? A.
Histidine.

Q. Which amino acid is optically inactive?

A. Glycine.

Q. What are the isomers of amino acids?

A. D and L varieties.

Q. What are natural amino acids?

A. Only L amino acids are seen in large quantities in nature.

Q. Can you name some substances where D-amino acids are seen?
A. D-amino acids are seen in cell walls of microorganisms and as constituents of certain
antibiotics such as gramicidin-S, polymyxin, actinomycin-D and valinomycin.

Q. What is meant by decarboxylation of an amino acid?

A. The carboxyl group is removed from the amino acids to form the corresponding
amine.

Q. Give examples of decarboxylation reactions.

A. Histidine to histamine; tyrosine to tyramine; tryptophan to tryptamine.

Q. What is produced when Glutamic acid is decarboxylated?

A. Gamma amino butyric acid or GABA.

Q. What is glutamine?
A. That is the amide of glutamic acid.

Q. What is an amide?
A. The extra carboxyl group (other thanÿalpha carboxyl) can combine with ammonia to
form the corresponding amide.

Q. How asparagines is produced?

A. Aspartic acid + ammonia will form asparagine.

Q. What is transamination?
A. The alpha amino group of amino acid can be transferred to alpha keto acid to form
the correspond ing new amino acid and alpha keto acid.
Q. Give an example of transamination reaction.
A. Glutamic acid + pyruvic acid alpha keto glutarate + alanine.

Q. What is the product of transamination reaction of pyruvate with glutamate?

A. Alanine and alpha keto glutarate.

Q. What is the biological significance of transamination reaction?

A. These are important for the interconversion of amino acids. Non-essential amino
acids are synthesized by this process.

Q. What is the clinical significance of transaminases?

A. Transaminases in blood are elevated in liver and heart diseases.

Q. What is the significance of SH groups in proteins?

A. The SH group of cysteine can form a disulfide (S-S) bond with another cysteine
residue. The two cysteine residues can connect two polypeptide chains by the
formation of interchain disulfide bonds.

Q. Glutathione is made up of which amino acids?

A. Glutamic acid, cysteine and glycine.

Q. Phosphorylation is taking place on which amino acid residue?

A. Serine.

Q. What is ninhydrin reaction?

A. All amino acids when heated with ninhydrin will give a pink colour.

Q. What is the importance of ninhydrin reaction?

A. It is used for qualitative test and quantitative estimation of amino acids. It is often
used for detection of amino acids in chromatography.

Q. Do proteins give a color with ninhydrin?

A. Proteins do not give a true color reaction; but N-terminal end amino group of protein
will react with ninhydrin, to produce a blue color.

Q. What is biuret reaction?

A. Cupric ions in alkaline medium form a violet colour with peptide bond nitrogen.

Q. Will amino acids give a positive biuret test?

A. No. This needs a minimum of two peptide bonds.

Q. What is the use of biuret reaction?

A. This reaction can be used for qualitative identification and quantitative estimation of
proteins.
Q. What is biuret?
A. The name is derived from the compound biuret, a condensation product of two
urea molecules, which also gives a positive color test.

Q. What is the basis of xanthoproteic test?

A. The ring systems in phenyl alanine, tyrosine and tryptophan will answer this test.

Q. The protein which does not answer the aldehyde test is.
A. Gelatin.

Q. How proteins are made up of? (Page 19)

A. Proteins are made by polymerisation of amino acids through peptide bonds.

Q. What is a peptide bond?

A. Alpha carboxyl group of one amino acid reacts with alpha amino group of another
amino acid to form a peptide bond or CO-NH bridge.

Q. What is a dipeptide?
A. Two amino acids are combined to form a dipeptide.

Q. How many peptide bonds are present in a tripeptide?

A. A tripeptide is a combination of three amino acids; so there are two peptide bonds.

Q. What is a polypeptide?
A. A combination of 10 to 50 amino acids is called as a polypeptide.

Proteins: Structure and Function

Q. What is the difference between a polypeptide and a protein?
A. A combination of 10 to 50 amino acids is called a polypeptide. By convention,
chains containing more than 50 amino acids are called proteins.

Q. What are the levels of organizations of proteins?

A. Proteins have primary, secondary, tertiary and quaternary levels of organisation.

Q. What is meant by primary structure of a protein?

A. It denotes the number and sequence of amino acids in the protein.

Q. What is the force that maintains the primary structure?

A. The primary structure is maintained by the covalent bonds of the peptide linkages.
Q. What are the salient features of a peptide bond?
A. The peptide bond is a partial double bond. The C-N bond is .trans. in nature and
there is no freedom of rotation because of the partial double bond character.

Q. What is the N-terminal end of a protein?

A. In a protein, at one end there will be one free alpha amino group. This end is called
the amino terminal (N-terminal) end and the amino acid contributing the ?-amino group
is named as the first amino acid.

Q. What are the names for the end amino acids of proteins.
A. The end where there is a free alpha amino group is called the amino terminal (N-
terminal) end. The other end of the polypeptide chain is called the carboxy terminal end
(C-terminal) where there is a free alpha carboxyl group.

Q. Can you give an example of a pseudopeptide?

A. Glutathione (gamma-glutamyl-cysteinyl-glycine). The pseudopeptide a peptide
bond formed by carboxyl group, other than that of alpha position.

Q. What are the salient structural features of insulin?

A. It has two polypeptide chains. These chains are held together by disulfide bridges.
Insulin has total 51 amino acids.

Q. What is pro-insulin?
A. Insulin is synthesised by the beta cells of pancreas as a prohormone, proinsulin is a
single polypeptide chain with 86 amino acids.

Q. What is mutation?
A. Amino acid change in the linear sequence is called a mutation.

Q. Can you give an example?

A. sickle cell anemia due to Haemoglobin S,

Q. What is the defect in HbS?

A. Normally the 6th amino acid in the beta chain is glutamic acid, this is replaced by
valine in the HbS molecule.

Q. Which are the forces that maintain the secondary, tertiary and quaternary structures
of a protein?
A. Hydrogen bonds, Electrostatic bonds, Vander Waals forces and Hydrophobic bonds.

Q. What are the salient features of alpha structure of proteins?

A. It is a right-handed spiral structure; each turn is formed by 3.6 amino acid
residues; it is major structural motif in globular proteins.
Q. Which will inhibit the formation of alpha helix?
A. Proline.

Q. What is meant by secondary structure of a protein?

A. Secondary structure denotes the configurational relationship between residues which
are about 3-4 amino acids apart. In other words, secondary level defines the
organisation at immediate vicinity of amino acids.

Q. What is meant by tertiary structure of a protein?

A. The tertiary structure denotes three dimensional structure of the whole protein. It
defines the steric relationship of amino acids which are far apart from each other in the
linear sequence.

Q. What is meant by a domain of a protein?

A. It is the term used to denote a compact unit of a protein. It generally represents a
functional unit.

Q. What is meant by quaternary structure of a protein?

A. Certain polypeptides will aggregate to form one functional protein. This is referred to
as the quaternary structure.

Q. Give some examples of proteins having quaternary structure.

A. Hemoglobin, lactate dehydrogenase, immunoglobulin.

Q. What are the reagents that are used for identifying the first amino acid in a protein?
A. Fluoro dinitro benzene, dansyl chloride, phenyl iso thio cyanate.

Q. Protein chains may be separated by what reagent?

A. 8 molar urea.

Q. What is meant by Ingram.s technique?

A. Protein digestion by trypsin, followed by two dimensional chromatography.

Q. It is otherwise known as what?

A. Finger printing of proteins or peptide mapping.

Q. Secondary structure of protein can be studied by what methods?

A. X-ray diffraction study, optical rotatory dispersion, and nuclear magnetic
resonance (NMR).

Q. What is iso-electric point of a protein?

A. At the iso-electric point, the number of anions and cations present on the protein
molecule will be equal and the net charge is zero.
Q. What are the characteristic features of iso-electric point?
A. At the pI value, the proteins will not migrate in an electrical field; solubility,
buffering capacity and viscosity will be minimum and precipitation will be maximum.

Q. What is the iso-electric pH of human albumin?

A. It is 4.7.

Q. How proteins are precipitated from solution?

A. Any factor which neutralises the charge or removes water of hydration will
cause precipitation of proteins.

Q. How albumin is precipitated?

A. By full saturation of ammonium sulfate or 28 % sodium sulfate.

Q. What will be precipitated by half-saturation of ammonium sulfate?

A. Globulins are precipitated by half-saturation of ammonium sulfate.

Q. Give an example of precipitation at iso-electric point.

A. Casein is precipitated when the solution is brought to iso-electric pH.

Q. What is the iso-electric pH of casein?

A. 4.6.

Q. Give some examples of anionic precipitating agents.

A. Tungstic acid, phosphotungstic acid, trichloro acetic acid, picric acid,
sulphosalicylic acid and tannic acid are protein precipitating agents.

Q. What are the features of denaturation?

A. The secondary, tertiary and quaternary structures are lost, but primary structure is
preserved. The functional activity is lost. The denature proteins are insoluble and easily
precipitated.

Q. What are the usual agents that cause denaturation of proteins?

A. Brief heating, urea, X-ray, ultraviolet ray, high pressure, vigorous shaking.

Q. What is heat coagulation?

A. When heated at iso-electric point, some proteins will denature irreversibly to produce
thick floating conglomerates called coagulum. This is called heat coagulation.

Q. Give examples of proteins that coagulate easily.

A. Albumin is easily coagulated, and globulins to a lesser extent.

Q. How proteins are classified?

A. They may be classified depending on the function or based on the physicochemical
characteristics or based on their nutritional value.
Q. What is the functional classification of proteins?
A. 1. Catalytic proteins, 2. Structural proteins, 3. Contractile proteins, 4. Transport
proteins, 5. Regulatory proteins or hormones, 6. Genetic proteins, and 7. Protective
proteins.

Q. Based on physiochemical properties, how are they classified?

A. Simple proteins, conjugated proteins and derived proteins.

Q. Give examples of simple proteins.

A. Albumins, globulins, protamines, prolamines, lectins, scleroproteins.

Q. Give examples of scleroproteins.

A. Collagen of bone, cartilage and tendon, keratin of hair, horn, nail and hoof.

Q. What are conjugated proteins?

A. Combinations of protein with a non-protein part is called prosthetic group.

Q. How are conjugated group subclassified?

A. Glycoproteins, lipoproteins, nucleoproteins, chromoproteins, phospho-proteins and
metallo-proteins.

Q. Give some examples of chromoproteins.

A. Hemoglobin, flavoproteins, visual purple.

Q. Give examples of phosphoproteins.

A. Casein of milk and vitellin of egg yolk.

Q. Where is this phosphate attached to proteins?

A. The phosphoric acid is added to the hydroxyl groups of serine and threonine
residues of proteins.

Q. What are lectins?

A. Plant proteins having specific carbohydrate binding site.

Q. Give an example of a nutritionally rich protein (first class protein).

A. Casein.

Q. Some proteins are called as poor proteins; why?

A. They lack in many essential amino acids and a diet based on these proteins will
not even sustain the body weight.

Q. Give an example of nutritionally poor protein.

A. Zein from corn lacks tryptophan and lysine.
Q. Which method of protein estimation is dependent on the intact peptide bond?
A. Biuret method.

Q. What is the advantage of biuret method?

A. The biuret method is simple one step process, and is the most widely used method
for plasma protein estimations.

Q. What is the disadvantage of biuret method?

A. The sensitivity of the method is less and is unsuitable for estimation of proteins in
milligram or microgram quantities.

Q. What is the basis of Lowry.s method of protein estimation?

A. This is based on the reduction of folin-ciocalteau phenol reagent (phosphomolybdic
acid and phosphotungstic acid) by the tyrosine and tryptophan residues of protein.

Q. Which component of the protein absorb UV light at 280 nm?

A. Indole ring of tryptophan.

Q. What is nephelometry?
A. Nephelometry is defined as the detection of light scattered by turbid particles in
solution.

Enzymology-I
Q. How are enzymes classified?
A. They are classified into five major classes.

Q. What are those classes?

A. Oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases.

Q. What is the function of oxidoreductases?

A. Transfer of hydrogen.

Q. Give an example of oxidoreducatase

A. Alcohol dehydrogenase.

Q. What is the function of transferases?

A. Transfer of groups other than hydrogen.

Q. Give an example of transferase

A. Hexokinase.

Q. What is the function of hydrolases?

A. Cleave bond after adding water.
Q. Give an example of a hydrolase.
A. Acetyl choline esterase.

Q. Peptidases are classified under which class of enzyme?

A. Hydrolases.

Q. What is the function of lyases?

A. Cleave bond without adding water.

Q. Which enzyme will add water to a double bond, without breaking the bond?
A. Hydratase.

Q. Give an example of lyase.

A. Aldolase.

Q. Give an example of isomerase.

A. Triose phosphate isomerase.

Q. What is the function of ligases?

A. ATP dependent condensation of two molecules.

Q. What is the difference between synthase and synthetase?

A. Synthetases are ATP-dependent enzymes catalysing biosynthetic reactions; they
belong to Ligases. Synthases are enzymes catalysing biosynthetic reactions; but they
do not require ATP directly; they belong to classes other than Ligases.

Q. Give examples of synthetases.

A. Carbamoyl phosphate synthetase, arginino succinate synthetase, PRPP synthetase,
glutamine synthetase.

Q. Give examples of synthases.

A. Glycogen synthase, ALA synthase, IMP synthase.

Q. What are co-enzymes?

A. Enzyme may contain a non-protein part, the co-enzyme. The co-enzyme is essential
for the biological activity of the enzyme. A co-enzyme is a low molecular weight organic
substance, without which the enzyme cannot exhibit any reaction. Co-enzyme accepts
one of the products of the reaction; and so act as a co-substrate.

Q. What is holo-enzyme?
A. When apo-enzyme and co-enzymes are added, holo-enzyme is produced. Fully
active enzyme is called Holo-enzyme.
Q. How are co-enzymes classified?
A. (a) Those taking part in reactions catalysed by oxidoreductases by donating or
accepting hydrogen atoms or electrons. (b) Those co-enzymes taking part in reactions
transferring groups other than hydrogen.

Q. Give some examples of co-enzymes involved in oxidoreductases.

A. NAD, NADP, FAD.

Q. What is the full form of NAD?

A. Nicotinamide adenine dinucleotide.

Q. What is FAD?
A. Flavin adenine dinucleotide.

Q. Give some examples of co-enzymes involved in reactions other than hydrogen

transfer.
A. Thiamine pyrophosphate, pyridoxal phosphate, biotin, co-enzyme A, ATP.

Q. What is the full form of ATP?

A. Adenosine triphosphate.

Q. What is the function of ATP?

A. It is the energy currency in the body. During the oxidation of food stuffs, energy is
released, a part of which is stored as chemical energy in the form of ATP. Other
reaction requiring energy are coupled with ATP.

Q. Name the enzymes containing copper

A. Superoxide dismutase, tyrosinase, cytochrome oxidase.

Q. Which metal is required for the action of Kinases?

A. Magnesium.

Q. Chloride ions activate which enzyme?

A. Amylase.

Q. Which enzyme contains molybdenum?

A. Xanthine oxidase.

Q. Name some iron containing enzymes.

A. Cytochrome oxidase, catalase, peroxidase, xanthine oxidase.

Q. What is Michaelis-Menten Theory ?

A. It is otherwise called enzyme-substrate complex theory. The enzyme combines with
the substrate, to form an enzyme-substrate complex, which immediately breaks down
to the enzyme and the product.
Q. What is Fischer.s theory?
A. It states that the three dimensional structure of the active site of the enzyme is
complementary to the substrate. Thus, enzyme and substrate fit each other like a key
and its lock.

Q. What is Koshland.s induced fit theory?

A. The substrate induces conformational changes in the enzyme, such that precise
orientation of catalytic groups is effected.

Q. What is active site of an enzyme?

A. That area of the enzyme where catalysis occurs is referred to as active site or active
center.

Q. What is meant by serine proteases?

A. Proteases (proteolytic enzymes) having a serine residue at its active center.

Q. Give an example of a serine protease

A. Trypsin, chymotrypsin, thrombin.

Q. Thermodynamically, how reactions are classified?

A. Exothermic, isothermic and endothermic reactions.

Q. What is exothermic reaction?

A. Here energy is released from the reaction, and therefore reaction essentially
goes to completion, e.g. urease enzyme, converting urea to ammonia + CO2 + energy.

Q. What is endergonic reaction?

A. Energy is consumed and external energy is to be supplied for these reactions. In the
body this is usually accomplished by coupling the endergonic reaction with an exergonic
reaction, e.g. Hexokinase reaction, Glucose + ATP ® Glucose-6-Phosphate + ADP.

Q. What are the salient features of enzyme kinetics?

A. Enzymes lower activation energy. They increase the chemical reaction, but do not
alter equilibrium of the reaction.

Q. What are the factors influencing enzyme reaction?

A. Enzyme concentration, substrate concentration, product concentration,
temperature, pH and presence of activators or inhibitors.

Q. What is Km value?
A. Substrate concentration (expressed in moles/L) at half-maximal velocity is the Km
value.
Q. What does it indicate?
A. It denotes that 50% of enzyme molecules are bound with substrate molecules at
that particular substrate concentration

Q. What is its significance?

A. Km is independent of enzyme concentration. Km value is thus constant for an
enzyme. It is the characteristic feature of a particular enzyme for a specific substrate.
Km denotes the affinity of enzyme to substrate. Thus, the lesser the numerical value
of Km, the affinity of the enzyme for the substrate is more.

Q. What is the use of assessing the Km value of an enzyme? What is the application?
A. Determination of Km value is also useful to understand the natural substrate of an
enzyme. Study of Km value will also differentiate the competitive and non-competitive
inhibitions.

Q. What is the effect of temperature on enzyme velocity?

A. The velocity of reaction increases when temperature is increased, reaches a
maximum and then falls (Bell-shaped curve)

Q. Why it falls?
A. when temperature is more than 50ºC, heat denaturation and consequent loss of
tertiary structure of protein occurs.

Q. What is the effect of pH on the activity of an enzyme?

A. Each enzyme has an optimum pH, on both sides of which the velocity will be
drastically reduced. The graph will show a bell-shaped curve.

Q. What is the explanation for the effect of pH?

A. The pH decides the charge on the amino acid residues at the active site. The net
charge on the enzyme protein would influence substrate binding and catalytic activity.

Q. What is the optimum pH of usual enzymes?

A. Usually enzymes have the optimum pH between 6 and 8.

Q. Are there any important exceptions for this general rule?

A. Pepsin (optimum pH 1-2), alkaline phosphatase (optimum pH 9-10) and Acid
phosphatase (4-5).

Q. What is zymogen?
A. It is otherwise called pro-enzyme. Inactive zymogen is activated by removal of a
piece of the pro-enzyme.

Q. Give an example of zymogen is activated?

A. By splitting a single peptide bond, and removal of a small polypeptide from
trypsinogen, the active trypsin is formed. This results in unmasking of the active centre.
Q. What is the significance of zymogen activation?
A. Gastro-intestinal enzymes are synthesised in the form of pro-enzymes, and only after
secretion into the alimentary canal, they are activated. This prevents autolysis of cellular
structural proteins. Coagulation factors are seen in blood as zymogen form, their
activation takes place only when necessity arises. This prevents intravascular
coagulation.

Q. What are the different types of inhibitions of enzyme activity?

A. Competitive inhibition, non-competitive inhibition, suicide inhibition, and allosteric
regulation.

Q. What are salient features of competitive inhibition?

A. Competitive inhibitor is a structural analogue. 2.It is reversible. 3. Km is increased. 4.
Vmax is not changed.

Q. Give examples of competitive inhibition.

A. Malonate inhibits succinate dehydrogenase.

Q. Give examples of clinical application of competitive inhibition.

A. Sulfonamide inhibits PABA incorporation in bacteria, and so acts as an antibacterial
agent. Methotrexate inhibits folate reductase system, dicoumarol inhibits vitamin K.

Q. What is the immediate treatment for methanol poisoning

A. Methanol is oxidised by alcohol dehydrogenase to formaldehyde which causes the
acute toxicity. Antidote to methanol poisoning is ethanol which is the natural substrate
for alcohol dehydrogenase. So ethanol is preferentially utilised.

Q. What are the salient features of non-competitive inhibition?

A. Non-competitive inhibitor has no structural similarity with the substrate. 2. It is
generally not reversible 3. Km is not changed. 4. Vmax is reduced.

Q. Give examples of non-competitive inhibition.

A. Di-isopropyl fluoro phosphate inhibits trypsin, fluoride inhibits and enolase.

Q. Iodo-acetate inhibits enzyme by reacting with which group at the active site of the
enzyme?
A. Sulfhydryl group.

Q. What is the mechanism of inhibitory action of Di-isopropyl fluoro phosphate?

A. It inhibits enzymes with serine in their active centres, e.g. acetylcholine esterase.

Q. What is suicide inhibition?

A. In suicide inhibition, the structural analogue is converted to a more effective
inhibitor with the help of the enzyme to be inhibited. The inhibitor makes use of the
enzyme.s own reaction mechanism to inactivate it.
Q. What is the other term for suicide inhibition?
A. Mechanism based inactivation.

Q. Give examples for suicide inhibition.

A. Ornithine decarboxylase (ODC) is inhibited by difluro methyl ornithine (DFMO).
Another example is Allopurinol which is oxidised by xanthine oxidase to alloxanthine
that is a strong inhibitor of xanthine oxidase.

Q. What is allosteric inhibition?

A. Allosteric enzyme has one catalytic site where the substrate binds and another
separate allosteric site where the modifier binds.

Q. What are the salient features of allosteric inhibition?

A. (1) The inhibitor is not a substrate analogue. (2) It is partially reversible when
excess substrate is added. (3) Km is usually increased. (4) Vmax is reduced. (5) Most
allosteric enzymes possess quaternary structure. They are made up of subunits.

Q. Give examples for allosteric inhibition.

A. ALA synthase, aspartyl trans-carbamoylase, HMG CoA reductase

Q. What is covalent modification?

A. It means, either addition of a group to the enzyme protein by a covalent bond; or
removal of a group by cleaving a covalent bond.

Q. Give some examples of covalent modification.

A. Glycogen synthase is inactive, in the phosphorylated state, whereas glycogen
phosphorylase is active when phosphorylated.

Q. What is meant by induction?

A. Induction is effected at the level of DNA. The inducer will relieve the repression on
the operator site and will remove the block on the biosynthesis of the enzyme
molecules.

Q. Give an example of induction.

A. Induction of lactose-utilising enzymes in the bacteria when the media contains
lactose in the absence of glucose. In humans, Tryptophan pyrrolase and
transaminases are induced by glucocorticoids. Glucokinase is induced by glucose.
ALA synthase is induced by barbiturates.

Q. What are constitutive enzymes?

A. Enzymes whose concentration in a cell is independent of inducer are called
constitutive enzymes.

Q. What is repression?
A. Repression acts at the gene level, the number of enzyme molecules is reduced in the
presence of repressor molecule.
Q. Give an example of repression.
A. The key enzyme of heme synthesis, ALA synthase is autoregulated by the heme by
means of repression.

Q. Give examples of multi-enzyme complexes.

A. Fatty acid synthase, pyruvate dehydrogenase, and alpha keto glutarate
dehydrogenase.

Q. What are the types of specificity shown by enzymes?

A. Absolute specificity, group specificity and streospecificity.

Q. Give an example for absolute specificity.

A. Urea is the only substrate for urease.

Q. Give an example for group specificity.

A. trypsin can hydrolyse peptide bonds formed by carboxyl groups of arginine or lysine
residues.

Q. What are iso-enzymes?

A. They are physically distinct forms of the same enzyme activity. They have
identical catalytic properties, but differ in structure.

Q. How to differentiate iso-enzymes.

A. Electrophoresis, heat stability, km value, inhibitor specificity, and tissue localization.

Q. Which is a functional enzyme in plasma?

A. They are actively secreted into plasma, and have some functions in the blood. For
example, enzymes of blood coagulation.

Q. What is non-functional enzymes in plasma?

A. They are coming out from cells due to normal wear and tear.

Enzymology-II Iso-Enzymes & Clinical Enzymology

Q. What is their clinical significance?
A. Their normal levels in blood are very low, but are drastically increased during
cell death (necrosis) or disease. Therefore, assays of these enzymes are very useful in
diagnosis of diseases.

Q. Lactate dehydrogenase has how many polypeptide subunits?

A. Four. It is a tetramer.

Q. Lactate dehydrogenase has how many iso-enzymes?

A. Five
Q. What are they? (Page 47)
A. H4, H3M, H2M2, M3H and M4 varieties, forming five iso-enzymes. All these five
forms are seen in all persons.

Q. How do you separate LDH iso-enzymes in laboratory?

A. By cellulose acetate electrophoresis at pH 8.6.

Q. LDH level in blood is increased in which conditions?

A. Myocardial infarction, hemolytic anemias, muscular dystrophy, carcinomas,
leukemias, and any condition which causes necrosis of body cells.

Q. How do you further investigate for myocardial infarction?

A. LDH-1 (H4) iso-enzyme is increased.

Q. What is flipped pattern?

A. Normally LDH-2 (H3M1) concentration in blood is greater than LDH-1 (H4), but this
pattern is reversed in myocardial infarction, this is called flipped pattern.

Q. What are the serum enzymes helpful in the diagnosis of myocardial infarction?
A. Lactate dehydrogenase (LDH) H4 iso-enzyme, creatine kinase (CK) CK MB iso-
enzyme and aspartyl transaminase (AST).

Q. Creatine kinase (CK) level in serum is increased in which conditions?

A. Myocardial infarction, muscular dystrophies.

Q. What is the advantage of CK estimation over LDH estimation to identify

myocardial infarction?
A. The CK level starts to rise within three hours of infarction. Therefore, CK estimation is
very use ful to detect early cases, where ECG changes may be ambiguous. The CK
level is not increased in hemolysis or in congestive cardiac failure; and therefore CK
has an advantage over LDH.

Q. What are the iso-enzymes of CK?

A. CK is a dimer, the subunits are called B for brain and M for muscle. Therefore, three
iso-enzymes are possible.

Q. What are the origins of the CK iso-enzymes?

A. Eighty percent of molecules in circulation are MM (CK3) variety of skeletal origin,
five percent in circulation are MB (CK2) from heart, one percent from brain (BB or
CK1) and fifteen percent CKmt from mitochondria.

Q. When do you estimate total CK and the iso-enzyme?

A. Estimation of total CK is employed in muscular dystrophies and CK-MB iso-enzyme
is estimated to identify myocardial infarction.
Q. What is the advantage of cardiac troponin I over other parameters to identify the
myocardial infarction?
A. Cardiac Troponin I is released into the blood within four hours after the onset of
cardiac symptoms, peaks at 12-16 hours and remains elevated for 5-9 days post-
infarction. Therefore, CTI is very useful as a marker at any time interval after the heart
attack. It is 75% sensitive index for myocardial infarction.

Q. What is the significance of AST?

A. It is significantly elevated in myocardial infarction and moderately elevated in liver
diseases.

Q. What is the significance of ALT?

A. Very high values are seen in acute hepatitis. Rise in ALT levels may be noticed
several days before clinical signs such as jaundice are manifested. Moderate
increase may be seen in chronic liver diseases such as cirrhosis, and malignancy in
liver.

Q. Alkaline phosphatase level in serum is elevated in which conditions?

A. Moderate increase is seen in hepatic diseases (infective hepatitis, alcoholic
hepatitis). High levels may be noticed in obstructive jaundice or cholestasis. Very
high levels are seen in bone diseases such as Paget.s disease, rickets, osteomala-
cia, osteoblastoma, metastatic carcinoma of bone.

Q. For alkaline phosphatase, how many iso-enzymes are present?

A. Six.

Q. What is Regan iso-enzyme?

A. It is the iso-enzyme of alkaline phosphatase, inhibited by phenylalanine. It is of
placental origin. It is elevated in about 15% cases of carcinoma of lung, liver and gut
and then named as Regan isoenzyme or carcinoplacental iso-enzyme.

Q. It is said that nucleotide phosphatase (NTP) is a better index of obstructive liver

disease than alkaline phosphatase (ALP), why?
A. ALP level is increased in both liver and bone diseases, but NTP is only in liver
diseases.

Q. Estimation of gamma glutamyl transferase is useful to detect which condition? A.

Alcohol abuse.

Q. What are the enzymes useful in diagnosing liver pathology?

A. ALT, ALP, GGT, NTP.

Q. Give the clinical implications of these enzymes.

A. In infective hepatitis, ALT level is increased; in alcohol abuse, GGT level is
increased; in obstructive jaundice, ALP level is increased.
Q. Serum acid phosphatase level is increased in which condition?
A. Prostate carcinoma.

Q. Total acid phosphatase may increase in some other conditions also; what are
they?
A. Prostate carcinoma, secondary metastasis in bones, per rectal examination,
intravascular hemolysis.

Q. In such conditions, iso-enzyme study is helpful or not?

A. Yes, tartarate labile iso-enzyme is specific for prostate carcinoma.

Q. What is the advantage of prostate specific antigen?

A. PSA is very specific for prostate carcinoma.

Q. What are the enzymes useful as tumour markers?

A. Regan iso-enzyme of ALP for lung tumour; tartarate labile iso-enzyme of ACP
and Prostate specific antigen (PSA) for prostate carcinoma; Neuron specific
enolase (NSE) for cancers of neuro-endocrine origin.

Q. Pseudo-cholinesterase deficiency is manifested as what?

A. Succinyl choline apnoea; prolonged apnea when succinyl choline is given as
anesthetic drug.

Q. Which enzyme deficiency is inherited as X- linked?

A. Glucose-6-phosphate-dehydrogenase.

Q. How the deficiency of GPD is manifested?

A. Drug induced hemolytic anemia.

Q. Acute pancreatitis can be diagnosed by estimating which enzymes?

A. Amylase and lipase.

Q. Name some enzymes that are used as therapeutic agents.

A. Asparaginase for leukemia, streptokinase to dissolve clots, and pepsin for
indigestion.

Methods of Separation and Purification of Biological

Compounds,Methods of Study of Metabolism
Q. What is meant by electrophoresis?
A. The term refers to the movement of charged particles through an electrolyte when
subjected to an electric field.
Q. What are the factors affecting the mobility in electrophoresis?
A. Net charge on the particles (pI of proteins), mass and shape of the particles, the pH
of the medium, strength of electrical field, and properties of the supporting medium.

Q. What are the types of electrophoresis?

A. Horizontal and vertical types.

Q. What are the supporting media used?

A. Filter paper, cellulose acetate, agar gel, agarose gel, starch gel and polyacrylamide
gel.

Q. Electrophoresis is commonly employed for what purpose in laboratory?

A. For serum electrophoresis and to see abnormalities in serum protein concentrations.

Q. What is the advantage of polyacrylamide gel?

A. It has a molecular sieving effect and so separation is very efficient.

Q. What is immuno-electrophoresis?
A. Here electrophoretic separation is followed by an antigen-antibody reaction.

Q. What is the principle of adsorption chromatography?

A. separation is based on differences in adsorption at the surface of a solid stationary
medium.

Q. What is the principle of partition chromatography?

A. the components of the mixture to be separated are partitioned between the two
phases depending on the partition co-efficient (solubility) of the particular substances.

Q. What are the common types of partition chromatography?

A. Paper chromatography and thin layer chromatography.

Q. What is the advantage of TLC over paper chromatography?

A. TLC needs lesser time, and separation is more effective.

Q. What is Rf value?
A. It is the ratio of the distance travelled by the substance (solute) to the distance
travelled by the solvent. The Rf value is a constant for a particular solvent system at a
given temperature.

Q. What is the basic principle of ion-exchange chromatography?

A. Here, the separation is based on electrostatic attraction between charged molecules
to oppositely charged groups on the ion exchange resins.

Q. What is the principle of gel filtration chromatography?

A. The separation is effected on the basis of the size of the molecules. It is otherwise
called molecular sieving.
Q. Give the principle of affinity chromatography.
A. The technique is based on the high affinity of specific proteins for specific chemical
groups.

Q. Give an example of affinity chromatography.

A. Separation and quantitation of glycated hemoglobin.

Q. What is the quickest method for separation of proteins?

A. HPLC.

Q. What is the principle of ultracentrifugation?

A. Large molecules can be sedimented at high centrifugal forces whereas small
molecules cannot. Rate of sedimentation depends on the size, shape and density of
solute particles.

Q. What is Svedberg unit? (Page 57)

A. Sedimentation constant is expressed in Svedberg (S) units.

Q. What are the uses of ultracentrifugation?

A. 1. Separation of subcellular organelles. 2. Separation of lipoproteins.
3. Determination of molecular weight of proteins.

Q. What are the methods used to determine the molecular weight of proteins?
A. (1) Ultracentrifugation, (2) Gel filtration and (c) PAGE (poly acrylamide gel
electrophoresis).

Q. What is the advantage of radio-immuno assay?

A. Very small quantities of substances could be accurately measured.

Q. What is the radio-active label used for RIA?

A. Iodine-125.

Q. What is the half life of Iodine-125?

A. About 60 days.

Q. What are the disadvantages of RIA, when compared to ELISA?

A. 1. Since radio-isotopes are used, only approved laboratories could take up the assay.
2. The shelf life of the reagent is short.

Q. What are the enzymes commonly used in ELISA technique.

A. Alkaline phosphatase (ALP) and horse radish peroxidase (HRP).

Q. How carbohydrates are classified?

A. Based on the number of the sugar units available, they are classified as
monosaccharides, disaccharides, oligosaccharides, and polysaccharides.
Q. What is a monosaccharide?
A. Molecules having only one actual or potential sugar group are called
monosaccharides.

Q. What is a polysaccharide?
A. They contain more than 10 sugar units.

Q. How are they combined together?

A. Through glycosidic linkages.

Q. How are monosaccharides further classified?

A. Sugars having aldehyde group are called aldoses and sugars with keto group are
ketoses.

Carbohydrates-I: Chemistry, Digestion and

Absorption
Q. Name some important monosaccharides.
A. Glucose, fructose, galactose, mannose.

Q. What are pentoses?

A. Monosaccharides with five carbon atoms.

Q. Name a few pentoses.

A. Arabinose, Xylose, Ribose.

Q. Which is the reference carbon atom in sugars?

A. Penultimate carbon atom.

Q. What is the difference between D and L sugars?

A. They are mirror images with reference to penultimate carbon atom.

Q. Which isomer is common in nature?

A. D variety of sugars are common in nature.

Q. Which is the most common monosaccharide in the body?

A. Glucose.

Q. What is the difference between glucose and galactose?

A. They are different with regard to the H and OH groups at the 4th carbon atom.
Galactose is the 4th epimer of glucose

Q. Galactose is present in which food?

A. Lactose is present in milk. Lactose contains galactose and glucose.
Q. What is epimerism?
A. When sugars are different from one another, only in configuration with regard to a
single carbon atom (other than the reference carbon atom), they are called epimers.

Q. Give an example.
A. For example, glucose and mannose are an epimeric pair which differ only with
respect to carbon atom 2. Similarly, galactose is the 4th epimer of glucose.

Q. Anomerism is produced with reference with which carbon atom?

A. Anomers are produced by the spatial configuration with reference to the first carbon
atom in aldoses and second carbon atom in ketoses.

Q. How alpha and beta forms of sugars are produced?

A. These are anomers. The difference lies in the spatial configuration with reference to
the first carbon atom in aldoses and second carbon atom in ketoses.

Q. What is the basis of mutarotation?

A. It is due to the anomeric carbon atom.

Q. What is the difference between glucose and fructose?

A. Glucose is an aldohexose, and fructose is a ketohexose.

Q. Name a ketose.
A. Fructose.

Q. What is the principle of Benedict.s test?

A. In alkaline medium, sugar will cause reduction of cupric ions, to form red coloured
precipitate.

Q. What is the composition of Benedict.s reagent.

A. It contains sodium carbonate, copper sulfate and sodium citrate. In the alkaline
medium provided by sodium carbonate, the copper remains as cupric hydroxide.
Sodium citrate acts as a stabilizing agent to prevent precipitation of cupric hydroxide.

Q. Benedict.s test is commonly employed for what?

A. To detect the presence of glucose in urine.

Q. Name a few reducing sugars.

A. Glucose, fructose, mannose.

Q. Keto group is non-reducing, but fructose reduces Benedict.s solution, what is the
cause for this anomaly?
A. In alkaline medium, ketone group is converted to aldehyde, through enediol
formation.
Q. In the case of sugars, which of the properties go hand in hand?
A. Reducing property, osazone formation and mutarotation.

Q. Glucose and fructose will form identical osazones, why?

A. The difference in glucose and fructose is dependent on the first and second carbon
atoms, and this is masked by the osazone formation.

Q. On oxidation of glucose, what are produced?

A. Glucuronic acid, gluconic acid and glucosaccharic acid.

Q. Reduction of glucose produces what?

A. Sorbitol.

Q. Name some deoxy sugars.

A. Deoxy ribose, fucose (deoxy galactose).

Q. Which is the stain used to identify deoxysugar?

A. Feulgen staining.

Q. Name some important disaccharides.

A. Sucrose, lactose, maltose.

Q. What is the glycosidic linkage in lactose?

A. Beta 1-4 linkage.

Q. What is the glycosidic linkage in sucrose?

A. 1-2 linkage.

Q. Which disaccharide has no free aldehyde or ketone group?

A. Sucrose.

Q. Glucose and fructose are reducing sugars, but sucrose (containing glucose and
fructose) is a non-reducing sugar, why?
A. Because the glycosidic linkage in sucrose involves 1st carbon of glucose and 2nd
carbon of fructose, so both reducing groups are masked.

Q. Hydrolysis of maltose will give rise to what ?

A. Two glucose units.

Q. Which is the sugar found in milk?

A. Lactose.

Q. What are the component monosaccharides of lactose?

A. Galactose and glucose.
Q. Sucrose consists of what monosaccharides?
A. Glucose + fructose.

Q. Name reducing disaccharides.

A. Lactose and maltose.

Q. How polysaccharides are classified?

A. Homopolysaccharides (homoglycans) and heteropolysaccharides (heteroglycans).

Q. What is a homopolysaccharide?
A. They are composed of single kind of monosaccharides.

Q. Give examples of homopolysaccharides.

A. Starch, and glycogen.

Q. What are heteropolysaccharides?

A. They are composed of two or more different monosaccharides.

Q. What are the characteristics of glycogen?

A. It is composed of glucose units. It is the stored form of carbohydrate in animal
kingdom. It has a highly branched structure.

Q. What is the reserve carbohydrate in plant kingdom?

A. Starch.

Q. What is the end product of action of pancreatic amylase on starch?

A. Maltose.

Q. Cellulose and starch are polysaccharides made of glucose, but cellulose cannot
be digest by human beings, why?
A. Cellulose contains beta 1,4 linkages, which cannot be digested by human enzymes.

Q. What is inulin?
A. It is a homopolysaccharide, composed of fructose units.

Q. What is the use of inulin?

A. It is used to find renal clearance and glomerular filtration rate.

Q. Give examples of heteropolysaccharides.

A. Agar, hyaluronic acid, heparin, chondroitin sulfate.

Q. What are mucopolysaccharides?

A. They contain uronic acid and amino sugars.

Q. Which heteropolysaccharide does not contain uronic acid?

A. Keratan sulfate.
Q. Hyaluronic acid is seen in which tissues?
A. Connective tissue, synovial fluid, tendons, vitreous humor.

Q. What is the difference between glycoprotein and mucoprotein?

A. If the carbohydrate content is less than 10%, it is called a glycoprotein. If the
carbohydrate content is more than 10% it is a mucoprotein.

Q. The rate of absorption of sugars in intestine is highest for which monosaccharide?

A. Absorption rate of galactose is more than glucose, while fructose is absorbed at a
lesser rate than glucose.

Q. Glucose is absorbed at the luminal side of gastro intestinal cells by which

mechanism?
A. Carrier mediated co-transport with sodium, named as sodium dependent glucose
transporter (SGluT).

Q. How glucose is released from intestinal cells into the blood stream?
A. Glucose transporter type 2 (GluT2) .

Q. How glucose is taken up by cells from blood stream?

A. In tissues GluT2 is involved in absorption of glucose from blood.

Q. What is the importance of GluT4?

A. It is the glucose transporter present in muscle and adipose tissues. Insulin induces
these transporters. In diabetes mellitus, entry of glucose into muscle is decreased,
because GluT4 is reduced in insulin deficiency.

Q. What is the glucose sensor in the beta cells of pancreas?

A. GluT2 acts as the glucose sensor mechanism, for the controlled supply of insulin into
blood stream.

Carbohydrates-II: Major Metabolic Pathways of

Glucose, Glycolysis, Gluconeogenesis, Glycogen
Metabolism
Q. What is glycolysis?
A. In this pathway, glucose is converted to pyruvate or lactate, along with production of
a small quantity of energy.

Q. In which condition pyruvate is produced, and when lactate?

A. In aerobic condition pyruvate is produced. When oxygen is lacking, lactate is
produced.
Q. What is the significance of Glycolysis?
A. It is the only pathway that is taking place in all the cells of the body. Glycolysis is the
only source of energy in erythrocytes. Moreover, anaerobic glycolysis forms the
major source of energy in actively contracting muscles.

Q. What is hexokinase?
A. Hexokinase is the first step in the glycolysis pathway. It phosphorylates glucose to
glucose-6-phosphate.

Q. What is glucokinase?
A. The reaction is similar to hexokinase. But glucokinase is present only in liver, acts
specifically on glucose, and is active when glucose level in blood is increased after a
food.

Q. Which tissues prefer anaerobic glycolysis?

A. RBCs, exercising muscle, and cancer cells.

Q. What is the importance of phospho fructokinase?

A. It is the key enzyme (rate limiting enzyme) of the pathway. It is an irreversible
reaction.

Q. What is the substrate for aldolase reaction?

A. Fructose-1,6-bisphosphate.

Q. During glycolysis, energy is produced during which steps?

A. Step 5, glyceraldehyde-3-phosphate to 1,3- bisphospho glycerate, Step 6, 1,3-
bis phosphoglycerate to 3-phospho glycerate, and Step 9,Phospho enol pyruvate to
pyruvate.

Q. Fluoride ions inhibit which enzyme?

A. Enolase.

Q. What is the importance of the above inhibition?

A. Fluoride is used to prevent glycolysis, as preservative for blood before glucose
estimation.

Q. NAD is reduced to NADH in which reaction ofglycolysis?

A. Glyceraldehyde-3-phosphate dehydrogenase reaction.

Q. NADH is oxidised to NAD in which reaction of glycolysis?

A. Lactate dehydrogenase reaction.

Q. What are substrate level phosphorylations in glycolysis?

A. 1,3-bisphospho glycerate kinase (step 6) and pyruvate kinase (step 9).
Q. What is the purpose of lactic acid production under anaerobic conditions?
A. NADH generated in the 5th step has to be oxidised to NAD+. This can be done
by oxygen. But when oxygen is lacking, the 5th step has to be coupled with the 10th
step for regeneration of NAD.

Q. As the end product of glycolysis, pyruvate and NADH are formed. During
anaerobiasis, this NADH is reconverted to NAD+ by what mechanism?
A. Lactate dehydrogenase reaction.

Q. As the end product of glycolysis, pyruvate and NADH are formed. During aerobic
conditions, this NADH is reconverted to NAD+ by what mechanism?
A. Oxygen.

Q. What is Cori.s cycle?

A. During exercise, lactate is produced in muscle. This lactate diffuses into the
blood. Lactate then reaches liver, where it is oxidised to pyruvate. It is then taken up
through gluconeogenesis pathway, and becomes glucose. This glucose can enter into
blood and then taken to muscle. This cycle is called Cori.s cycle, or lactic acid cycle.

Q. What is the purpose of Cori.s cycle?

A. By this means, the lactate is efficiently reutilized by the body.

Q. Why lactate is transported from muscle to liver?

A. Oxygen is limited in muscle, so lactic acid could not be made to pyruvate in muscle.
So, it is transported to liver, where it is made to pyruvate and then to glucose.

Q. What are the inhibitors of phosphofructokinase?

A. ATP, Citrate, Glucocorticoids.

Q. What are the activators of phospho fructo kinase?

A. AMP, Fructose-2,6-bisphosphate, Fructose-6-phosphate.

Q. What are key glycolytic enzymes?

A. Glucokinase, Phospho fructo kinase, Pyruvate kinase.

Q. What is the action of insulin on glycolysis?

A. Insulin stimulates glycolysis.

Q. What is the net yield of ATP from one glucose molecule during anaerobic glycolysis?
A. 2 ATP.

Q. In aerobic glycolysis, the net yield from one glucose molecule is how much?
A. 8 ATP.

Q. During complete oxidation, what is the net yield of ATP from one glucose molecule?
A. 38 ATP.
Q. How many ATPs are generated per one rotation of the citric acid cycle?
A. 12 ATP.

Q. What is the function of 2,3-bisphospho glycerate?

A. When combined with hemoglobin, 2,3-BPG reduces the affinity towards oxygen.

Q. What are the steps in which carbon dioxide is produced from a glucose molecule?
A. Pyruvate dehydrogenase, isocitrate dehydrogenase, alpha keto glutarate
dehydrogenase.

Q. What are the co-enzymes necessary for oxidative decarboxylation of pyruvate?

A. Thiamine pyrophosphate, NAD, FAD, Lipoic acid, Co-enzyme A.

Q. What is pyruvate dehydrogenase?

A. The enzyme catalysing the reaction, pyruvate to acetyl CoA.

Q. What is pyruvate carboxylase?

A. The enzyme catalysing the reaction, pyruvate to oxaloacetate.

Q. What is pyruvate kinase?

A. It catalyses the reaction, phospho enol pyruvate to pyruvate.

Q. There is no net synthesis of glucose from fatty acids, why?

A. Pyruvate to acetyl CoA is a totally irreversible reaction.

Q. Which enzyme irreversibly channels glucose to energy production, rather than

retaining glucose for blood sugar regulation?
A. Pyruvate dehydrogenase is an irreversible reaction.

Q. Pyruvate is converted to acetyl CoA by which enzyme?

A. Pyruvate dehydrogenate.

Q. What is gluconeogenesis?
A. Production of glucose from non-carbohydrate sources.

Q. What are those non-carbohydrate sources? (What are the substrates for
gluconeogenesis?).
A. Glucogenic amino acids and lactate.

Q. What are the key gluconeogenic enzymes?

A. Pyruvate carboxylase, Phospho enol pyruvate carboxy kinase, Fructose-1,6-
bisphosphatase and Glucose-6-phosphatase.

Q. Pyruvate carboxylase reaction (pyruvate to oxaloacetate) needs which co-enzyme?

A. Biotin and ATP.
Q. Malate shuttle is used for what purpose?
A. Reactions of gluconeogenesis are taking place in cytosol. Hence the oxaloacetate
has to be transported from mitochondria to cytosol. This is achieved by the malate
shuttle.

Q. Gluconeogenesis is taking place in which tissue?

A. Liver.

Q. How many ATP molecules are required to convert two molecules of pyruvate into
glucose?
A. Six.

Q. Blood glucose level can be raised by gluconeogenesis only by liver, why?

A. Glucose-6-phosphatase is present only in liver.

Q. Muscle glycogen will not serve as a precursor of blood sugar, why?

A. Glucose-6-phosphatase is absent in muscle.

Q. Which amino acids are both ketogenic and glucogenic?

A. Tyrosine and tryptophan.

Q. What will inhibit gluconeogenesis?

A. Insulin.

Q. What will stimulate gluconeogenesis?

A. Glucagon and glucocorticoids.

Q. What is the significance of gluconeogenesis?

A. Gluconeogenesis is necessary to maintain blood glucose level especially under
conditions of starvation.

Q. What is glycogenolysis?
A. Degradation of glycogen to glucose.

Q. What is the main enzyme for glycogenolysis?

A. Glycogen phosphorylase.

Q. Which hormones enhance glycogenolysis?

A. Adrenaline and glucagon causes glycogenolysis.

Q. What is the mechanism of action of adrenaline?

A. Adrenaline increases cyclic AMP level which activates glycogen phosphorylase.

Q. In the glycogen synthesis, which is the active glucose derivative?

A. UDP-glucose.
Q. Adrenaline acts on which enzyme?
A. Glycogen phosphorylase.

Q. What will activate glycogen phosphorylase?

A. Epinephrine, glucagon, cyclic AMP.

Q. Which is the defective enzyme in von Gierke.s disease (glycogen storage disease
type I)?
A. Glucose-6-phosphatase.

Q. What are the characteristic clinical features of von Gierke.s disease?

A. Fasting hypoglycemia, which does not respond to adrenaline is very characteristic.

Q. What is the level of fasting blood sugar in a normal person?

A. 70-110 mg/dl.

Q. Which hormone is hypoglycemic?

A. Insulin.

Q. What are the major actions of insulin?

A. Insulin decreases blood sugar, it stimulates glycolysis, inhibits gluconeogenesis,
enhances glycogen synthesis and inhibits lipolysis.

Q. What are the anti-insulin (hyperglycemic) hormones?

A. Glucagon, adrenaline, corticosteroids, growth hormone.

Q. What are the major actions of glucagon?

A. Promotes glycogenolysis, enhances gluconeogenesis, depresses glycogen
synthesis, inhibits glycolysis.

Carbohydrates-III:Regulation of Blood Sugar,

Insulin and Diabets Mellitus
Q. What is the best method for glucose estimation?
A. Glucose oxidase peroxidase (GOD-POD) method.

Q. What is the major indication for doing an oral glucose tolerance test (OGTT)?
A. Patient has symptoms suggestive of diabetes mellitus, but fasting blood sugar value
is inconclusive (between 100 and 126 mg/dl).

Q. What are the precautions to take before OGTT?

A. Patient should have a good carbohydrate diet for three days prior to the test. Patient
should avoid insulin and oral antidiabetic drugs. Patient should fast overnight. Patient
should not take any breakfast.
Q. What is the glucose load dose?
A. Seventy five gram anhydrous glucose (82.5 g of glucose monohydrate) in 250-300 ml
of water.

Q. What precaution would you take in giving the glucose load?

A. In order to prevent vomiting, patient is asked to drink it slowly (within about 5
minutes). Flavouring of the solution will also reduce the tendency to vomit.

Q. What are the criteria for diagnosing diabetic mellitus?

A. Fasting plasma sugar is more than 126 mg/dl, on more than one occasion. 2. Or, if 2-
hour post-glucose load value of OGTT is more than 200 mg/dl (even at one occasion).
3. Or, if both fasting and 2-hour values are above these levels, on the same occasion.

Q. Can you diagnose diabetes on the basis of random blood estimations?

A. Diabetes is diagnosed, if the random plasma sugar level is more than 200 mg/dl, on
more than one occasion. Diagnosis should not be based on a single random test
alone, it should be repeated.

Q. When a standard oral glucose tolerance test was done, the blood glucose levels of
the patient were found as:0 min = 130 mg/dl and 120 min = 220 mg/dl. What will be your
diagnosis?
A. Diabetes mellitus.

Q. What is impaired glucose tolerance (IGT)?

A. When fasting plasma glucose level is between 110 and 126 mg/dl and 2-hour post-
glucose value is between 140 and 200 mg/dl.

Q. When a standard oral glucose tolerance test was done, the blood glucose levels of
the patient were found as:0 min = 120 mg/dl, 120 min = 160 mg /dl. What is your
diagnosis?
A. Impaired glucose tolerance.

Q. What you will do for such persons?

A. Such persons need careful follow up because IGT progresses to frank diabetes at
the rate of 2% patients per year.

Q. What is impaired fasting glycemia (IFG).

A. In this condition, fasting plasma sugar is abnormal (between 110 and 126 mg/dl), but
the 2-hour post-glucose value is within normal limits (less than 140 mg/dl).

Q. What you will do for such persons?

A. These persons need no immediate treatment, but are to be kept under constant
check-up. They are at increased risk for development of diabetes or cardiovascular
diseases.
Q. What is gestational diabetes mellitus (GDM)?
A. This term is used when carbohydrate intolerance is noticed, for the first time, during a
pregnancy. If the fasting value is more than 126 mg%, it is taken as gestational
diabetes.

Q. If a known diabetic patient, who becomes pregnant, will you include her in the
category of GDM?
A. No.

Q. What is the clinical significance of GDM?

A. Women with GDM are at increased risk for subsequent development of frank
diabetes. GDM is associated with increased birth weight of child and increased
incidence of neonatal mortality.

Q. After delivery, what you will do for a person with GDM?

A. After the child birth, the women should be re assessed and accordingly classified as
having either diabetes mellitus or normal glucose tolerance, based on the results of a
fresh OGTT.

Q. What are other conditions which may cause impaired glucose tolerance?
A. Alimentary glucosuria, renal glucosuria.

Q. What is renal glucosuria?

A. Here glucose is excreted in urine due to a lowering of renal threshold. The blood
sugar levels are within normal limits.

Q. What is normal renal threshold for glucose?

A. 180 mg/100 ml.

Q. What are the reducing substances seen in urine?

A. Glucose, fructose, lactose, galactose, pentoses, ascorbic acid, glucuronides.

Q. What is transient glucosuria?

A. It may occur in some people due to emotional stress. Excessive secretion of
catecholamines will produce hyperglycemia and resultant glucosuria. Once theÿstress is
removed, the glucosuria disappears.

Q. What is fructosuria?
A. Presence of fructose in urine. It is due to the deficiency of fructokinase or aldolase B

Q. What is lactosuria?
A. It is observed in the urine of normal women during 3rd trimester of pregnancy and
during lactation.
Q. What is the clinical importance of lactosuria?
A. The condition is harmless. But it is important to distinguish lactosuria from glucosuria
when gestational diabetes mellitus is suspected.

Q. What is the test for reducing sugars in urine?

A. Benedict.s test.

Q. What are the pathways stimulated by insulin?

A. Glycolysis, glycogen synthesis, HMP shunt pathway, lipogenesis.

Q. Name important enzymes that are stimulated by Insulin.

A. Phospho fructo kinase, glycogen synthase, glucose-6-phosphate dehydrogenase,
acetyl CoA carboxylase.

Q. What are the pathways inhibited by insulin?

A. Gluconeogenesis, glycogenolysis, lipolysis, ketogenesis.

Q. What are the important enzymes inhibited by insulin?

A. Glucose-6-phosphatase, glycogen phosphorylase, hormone sensitive lipase.

Q. Where is insulin synthesised?

A. Beta cells of langerhans of pancreas.

Q. What is proinsulin?
A. Insulin is synthesised as a large single polypeptide. Middle part of it is then removed,
to form the A and B chains of insulin.

Q. What is C peptide?
A. It is the part removed from proinsulin during the maturation of insulin molecule.

Q. What is the clinical significance of C peptide?

A. Sometimes measurement of endogenous insulin may be difficult because of the
presence of antibodies against insulin in the circulation. Then measurement of C-
peptide is useful.

Q. What are the salient structural features of insulin?

A. Insulin is a protein hormone with two poly peptide chains, the A chain with 21 amino
acids and the B chain with 30 amino acids are joined together by a pair of disulfide
bonds. It has a total of 51 amino acids.

Q. How is insulin secretion controlled?

A. Glucose is the major stimulant of insulin secretion.
Q. How glucose stimulates insulin secretion?
A. The beta cells have GluT 2 receptors, these act as sensor mechanism for glucose
level. The insulin secretion is controlled by a cyclic AMP-mediated mechanism. Cyclic
AMP along with calcium causes the insulin secretion.

Q. What is the effect of insulin on glucose uptake of cells?

A. Insulin facilitates the membrane transport of glucose in most of tissues, especially in
muscles and adipose tissue. This is by glucose transporter,GIuT4. But glucose
uptake by GlT2 is independent of insulin, it is seen in liver and brain.

Q. Maximum glucose utilisation is seen in which tissue?

A. At basal rates, brain utilises 60% of sugar oxidised.

Q. What is the mechanism of action of insulin?

A. Insulin acts by binding to membrane receptor, on the target cells.

Q. What is the structural feature of insulin receptor?

A. Insulin receptor has four subunits, two alpha and two beta subunits. The alpha units
are located on the extracellular side, to which insulin binds. The beta subunits are
towards cytoplasmic side. Beta subunit has tyrosine kinase activity.

Q. How diabetes mellitus is classified?

A. Type 1 and type 2.

Q. What are the characteristic features of type 1, diabetes mellitus?

A. Here circulating insulin level is deficient. These patients are dependent on insulin
injections. Onset is during adolescence. Rapid loss of body weight is observed.
They are more prone to developing ketosis.

Q. What about type 2 diabetes mellitus?

A. Most of the patients belong to this type. Here circulating insulin level is normal, but
there is a relative insulin deficiency. It is commonly seen in individuals above 40 years.
These patients are less prone to developing ketosis.

Q. What is maturity onset diabetes of young (MODY)?

A. It is due to defective glucokinase.

Q. What are the cardinal symptoms of diabetes mellitus?

A. Polyuria, polydypsia, polyphagia and weight loss.

Q. What is the reason for polyuria in diabetes mellitus?

A. When the blood glucose level exceeds the renal threshold glucose is excreted in
urine. Due to osmotic effect, more water accompanies the glucose.
Q. What is the reason for polydypsia in diabetes mellitus?
A. To compensate for this loss of water, thirst centre is activated, and more water is
taken (polydypsia).

Q. What is the reason for weight loss in diabetes mellitus?

A. The loss and ineffective utilisation of glucose leads to breakdown of fat and
protein.ÿThis would lead to loss of weight.

Q. What is the reason for polyphagia in diabetes mellitus?

A. To compensate the loss of glucose and protein, patient takes more food.

Q. What are the acute complications of diabetes mellitus?

A. Keto acidosis, hyperosmolar non-ketotic coma, lactic acidosis.

Q. What are the chronic complications of diabetes mellitus?

A. Thrombosis, paralysis, gangrene, micro-angiopathy, nephrosclerosis, cataract,
peripheral neuropathy.

Q. What is micro-albuminuria?
A. Albumin 50 to 300 mg/day in urine. It is a predictor of progressive renal damage,
atherosclerotic diseases and cardiovascular mortality. Albumin more than 300
mg/day indicates overt diabetic nephropathy.

Q. What is the cause for cataract in diabetes mellitus?

A. Early development of cataract of lens is due to the increased rate of sorbitol
formation, caused by the hyperglycemia.

Q. What is the difference between glycosylation and glycation?

A. Enzymatic addition of any sugar to a protein is called .glycosylation. while non-
enzymatic process is termed .glycation..

Q. What is the basis of glycation?

A. When there is hyperglycemia, proteins in the body may undergo glycation. It is a non-
enzymatic process. Glucose is added to the N-terminal amino group of proteins.

Q. What is the significance of glycated hemoglobin?

A. The determination of glycated hemoglobin is not for diagnosis of diabetes mellitus,
but for monitoring the response of treatment. It is unaffected by recent food intake or
recent changes in blood sugar levels. An elevated glycohemoglobin indicates poor
control of diabetes mellitus. The risk of retinopathy and renal complications are pro-
portionately increased with elevated glycatedhemoglobin.
Carbohydrates-IV: Other Metabolic Pathways
(HMP Shunt Pathway,Fructose, Galactose, Glucuronic
Acid, Alcohol)
Q. HMP shunt pathway use how much glucose?
A. About 10% of glucose molecules per day are entering in this pathway.

Q. What are the tissues in which HMP shunt pathway is significant?

A. Liver, adipose tissue, RBC, adrenal cortex, ovary, testis, mammary gland, lens.

Q. Which is the key enzyme of hexose monophosphate shunt pathway?

A. Glucose-6-phosphate dehydrogenase.

Q. What is the hormonal control over HMP shunt pathway?

A. Insulin stimulates the pathway by activating the key enzyme.

Q. Which enzyme generates NADPH?

A. Glucose-6-phosphate dehydrogenase.

Q. What is the purpose of HMP shunt pathway?

A. It generates NADPH.

Q. What is the use of NADPH in biological systems?

A. For reductive biosynthesis.

Q. What reductive biosynthesis pathways need NADPH?

A. Fatty acid biosynthesis, synthesis of cholesterol, steroid hormones.

Q. Apart from reductive synthesis, NADPH is used for what purpose?

A. It is necessary to keep the integrity of RBC membrane, it is needed for keeping
glutathione in reduced state, it is required for keeping transparency of lens, it is
necessary for superoxide production inside macrophages.

Q. What about ATP generation? NADPH is used for that?

A. No. NADPH is not used for ATP generation.

Q. Apart from NADPH generation, is there any other purpose for the HMPshunt
pathway?
A. The pathway is required for the synthesis of ribose, the pentose phosphates are
necessary for nucleotide (DNA and RNA) synthesis.

Q. What is the manifestation of glucose-6-phosphate dehydrogenase deficiency?

A. Drug induced hemolysis and met-hemoglobinemia.
Q. Acute hemolytic episode after administration of antimalarial drug is due to what?
A. Deficiency of glucose-6-phosphate dehydrogenase.

Q. What is the most common enzyme deficiency in man?

A. Glucose-6-phosphate dehydrogenase deficiency.

Q. What is the mode of hereditary transmission of GPD deficiency?

A. It is transmitted as an x-linked recessive character.

Q. Is there any advantage of the abnormal gene?

A. The geographical distribution of GPD deficiency correlates well with the malarial
endemicity. The GPD deficiency offers resistance to malarial infection.

Q. What is the clinical significance of transketolase enzyme?

A. The transketolase reaction is measured in RBCs as an index of the thiamine status of
an individual.

Q. Abnormal transketolase leads to what clinical condition?

A. The occurrence of Wernick.s encephalopathy (seen in alcoholics and in thiamine
deficiency) is due to a genetic defect in the enzyme transketolase. It occurs owing to the
enzyme having low binding capacity for TPP.

Q. Transketolase activity is decreased in the deficiency what?

A. Thiamine pyrophosphate (TPP).

Q. What is the purpose of uronic acid pathway?

A. It is used for conjugation of bilirubin, steroids, synthesis of gluco-saminoglycans.

Q. In lower animals, uronic acid pathway is used for what purpose?

A. For synthesis of ascorbic acid (vitamin C).

Q. What is essential pentosuria?

A. Excretion of pentose (L-xylulose) in urine due to the deficiency of xylitol
dehydrogenase.

Q. What is its importance?

A. It does not produce any harm. But it gives a positive reaction to Benedict.s test, so it
should be differentiated from diabetes mellitus.

Q. What is the clinical significance of polyol pathway?

A. The elevated level of sorbitol has been implicated in the development of neuropathy,
cataract and retinopathy in diabetes mellitus.

Q. Fructokinase catalyses which reaction?

A. Fructose to fructose-1-phosphate.
Q. What is fructose intolerance?
A. Due defective aldolase-B, fructose-1-phosphate accumulates. This leads to
accumulation of glycogen in liver, and hypoglycemia.

Q. Free fructose is seen in which body fluid?

A. Seminal plasma.

Q. This fructose is produced by which pathway?

A. Polyol pathway of glucose.

Q. What is the clinical application of fructose estimation in semen?

A. Fructose is secreted by seminal vesicles. A block in seminal vessels is indicated by
the absence of fructose in semen.

Q. What is fructosuria?
A. It is a benign metabolic defect due to deficiency of fructokinase. Urine gives
positive Benedict.s test, and so it should be differentiated from diabetes mellitus.

Q. Neonatal hypoglycemia is seen in which conditions?

A. Glycogen storage disease, type I, galactosemia, fructose intolerance.

Q. What are the features of galactosemia?

A. Congenital cataract, mental retardation, neonatal hypoglycemia,
hepatosplenomegaly, positive Benedict.s test.

Q. Congenital cataract is seen in which condition?

A. Galactosemia.

Q. Galactosemia is due the absence of which enzyme?

A. Galactose-1-phosphate uridyl transferase.

Q. What is the treatment policy in galactosemia?

A. Lactose free diet is given for first five years of life.

Q. Why five years, why life-long treatment is not required?

A. By five years, the alternate pathway (galatose-1-phosphate pyrophosphorylase)
becomes active.

Q. Why excessive intake of alcohol produces lactic acidosis?

A. During alcohol oxidation, NADH is generated, which converts pyruvate to lactate.

Q. Why excessive intake of alcohol produces hypoglycemia?

A. Because ethanol inhibits gluconeogenesis.

Q. What are the results of chronic alcoholism?

A. Polyneuropathy, fatty liver, cirrhosis, Werneck.s encephalopathy.
Q. How N-acetyl neuraminic acid (sialic acid) is synthesised?
A. N-acetyl mannosamine-6-phosphate + phosphoenol pyruvate.

Q. In glycoproteins, carbohydrate residues are attached to which group of the

polypeptide chain?
A. Hydroxyl group of serine or threonine.

Q. Increased glucosaminoglycans in urine is seen in which condition?

A. Mucopolysaccharidosis.

Lipids-I: Chemistry, Digestion and Absorption of

Lipids
Q. How lipids are classified?
A. Simple, compound and derived.

Q. Classify fatty acids.

A. Depending on the total number of carbon atoms, they are classified as even chain
and odd chain.

Q. Which type is prevalent in human body?

A. Even chain fatty acids.

Q. Fatty acids are classified in any other manner?

A. They are also classified as saturated or unsaturated fatty acids.

Q. What fatty acids are generally present in human fat?

A. Mainly Oleic acid, then comes palmitic acid and linoleic acid.

Q. How many carbon atoms are present in oleic acid?

A. 18 carbon, with one double bond.

Q. Name some unsaturated fatty acids.

A. Oleic, linoleic, linolenic and arachidonic acids.

Q. Name some polyunsaturated fatty acids.

A. Linoleic, linolenic and arachidonic acids.

Q. What is the structure of linoleic acid?

A. 18 carbon, with two double bonds.

Q. What is the structure of linolenic acid?

A. 18 carbon with three double bonds.
Q. What is the structure of arachidonic acid?
A. 20 carbon with four double bonds.

Q. Which contains good quantity of PUFA?

A. Vegetable oils such as sunflower oil, ground nut oil.

Q. Which contains very low level of PUFA?

A. Coconut oil and animal fats.

Q. What is the advantage of storing energy as triglycerides in the body?

A. Space requirement is less, storage does not require water, can be mobilised
whenever required, capacity for storage is unlimited.

Q. What is saponification?
A. Hydrolysis of fat by alkali is called are saponification.

Q. Does saponification number of a fat molecule increase or decrease with the

molecular weight of the fat?
A. Decreases with increase in molecular weight of fat.

Q. Odour of rancid oil is due to what?

A. Partial oxidation of fatty acids, with formation of epoxides and peroxides of small
molecular weight fatty acids.

Q. Complete digestion of triacyl glycerol (triglyceride) in gastro intestinal tract needs

what enzymes?
A. Pancreatic lipase, co-lipase, isomerase and bile salts

Q. What is the function of pancreatic lipase?

A. Partial hydrolysis of triacyl glycerol. The products are 2-mono acylglycerol (2-MAG)
(?-monoglyceride) and two fatty acid molecule

Q. What is the function of isomerase?

A. Isomerase shifts the ester bond from position 2 to 1, this is then hydrolysed by the
lipase to form free glycerol and fatty acid.

Q. Will there be complete breakdown of triglyceride into fatty acid in the gastro intestinal
tract?
A. No, only partial digestion is possible.

Q. What are the final end products of digestion of triglyceride?

A. 2-monoacyl glyceride (78%), 1-monoacyl glyceride (6%), glycerol and fatty acids
(14%).

Q. How small chain fatty acids are absorbed?

A. Small chain and medium chain fatty acids (chain length less than 14 carbons) are
directly absorbed from the intestinal lumen into the portal vein and taken to the liver.
Q. How long chain fatty acids are absorbed?
A. Long chain fatty acids (chain length more than 14 carbons) are absorbed by forming
micelles with the help of bile salts.

Q. How bile salts help in the absorption of dietary lipids?

A. By emulsifying the lipids and producing micelles of lipids.

Q. What is the chemical name of bile salts?

A. Sodium glycocholate and sodium taurocholate.

Q. What are micelles?

A. The micelles are spherical particles with a hydrophilic exterior and hydrophobic
interior core. Monoglycerides, long chain fatty acids, cholesterol, phospholipids and
lysophospholipids are incorporated into molecular aggregates to form mixed
micelles.

Q. What happens to the micelles?

A. Fatty acids and monoacyl glycerides from the micelles passively diffuse into the
mucosal cell.

Q. What happens to the fatty acids in the mucosal cell?

A. Once inside the intestinal mucosal cell, the long chain fatty acids are re-esterified to
form triglycerides.

Q. What is the further fate of this triglyceride?

A. The triglyceride, along with phospholipids, apoproteins B48, and apo-A are
incorporated into chylomicrons. The chyle (milky fluid) from the intestinal mucosal
cells loaded with chylomicrons are transported through the lacteals into the thoracic
duct and then emptied into systemic circulation.

Q. What is the difference for absorption of short chain fatty acid?

A. Short and medium chain fatty acids do not need re-esterification. They directly
enter into blood vessels (Not to lacteals).

Q. Where will you find short and medium chain fatty acids?
A. They are seen in butter, ghee, coconut oil and mother.s milk.

Q. What happens to the bile salts of micelle?

A. The bile salts are left behind.

Q. What is enterohepatic circulation of bile salts?

A. They are separately reabsorbed from the ileum and returned to the liver to be re-
excreted again to gut.

Q. What is steatorrhea?
A. When excretion of fat in faeces is more than 6 g per day, it is called steatorrhea.
Q. What is it due to?
A. It is due to defective digestion as in chronic diseases of pancreas. In such cases,
unsplit fat is excreted in feces.

Q. What happens in defective absorption?

A. If the absorption alone is defective, most of the fat in faeces may be split fat, i.e. fatty
acids and monoglycerides.
Q. What is the cause for defective absorption of fat?
A. It may be due to diseases in intestinal mucosa, e.g. coeliac disease, sprue,
Crohn.s disease.

Q. Any other cause for defective absorption of fat?

A. Any condition leading to a deficiency of bile salts can also result in malabsorption of
fat. The most common causes are obstruction to biliary tract due to gall stones, tumours
of head of pancreas, enlarged lymph glands, etc.

Q. What is the line of management in defective absorption?

A. In such cases, triglycerides with short chain and medium chain fatty acids are
digested and absorbed properly, because they do not require micellerisation for
absorption. Since milk fat and coconut oil are made up of MCT, they are thera-
peutically useful in malabsorption syndromes.

Lipids-II: Metabolism of Fatty acids,Fatty acid

oxidation,Fatty acid synthesis,Lipolysis, Ketone bodies.
Q. How fatty acids are activated in preparation of oxidation?
A. Fatty acids are activated to their co-enzyme A (CoA) derivative.

Q. What is the enzyme for this activation?

A. Thiokinase or fatty acyl CoA synthetase.

Q. How much ATP is required for this reaction?

A. One molecule of ATP is hydrolysed to AMP and PPI. Thus two high energy bonds
are utilised in this reaction.

Q. What are the co-enzymes needed for fatty acid oxidation?

A. FAD and NAD.

Q. What is carnitine?
A. Carnitine is beta-hydroxy-gamma-trimethyl ammonium butyrate. It is synthesised
from lysine and methionine in liver and kidney.
Q. What is the function of carnitine?
A. Fatty acids are activated in the cytoplasm, but the beta-oxidation is in mitochondria.
The long chain fatty acyl CoA cannot pass through the inner mitochondrial membrane.
Therefore a transporter, carnitine is involved in transfer of fatty acids.

Q. What about medium and small chain fatty acids?

A. Medium chain fatty acids do not require carnitine for transport, so they are easily
oxidised.

Q. What is the net generation of ATP, when one molecule of palmitic acid (16
carbon) is oxidized completely?
A. 129.

Q. What are the products, during each cycle of beta oxidation of fatty acid?
A. Acetyl CoA, FADH2, and NADH.

Q. What are the energy producing steps in beta oxidation pathway?

A. Fatty acyl CoA dehydrogenase (FAD) and beta hydroxy fatty acyl CoA
dehydrogenase (NAD) steps.

Q. What is the product of beta oxidation of odd chain fatty acids?

A. Propionyl CoA.

Q. What is the further metabolism of propionyl CoA?

A. Propionyl CoA is first carboxylated to methyl malonyl CoA and then to form
succinyl CoA. The succinyl CoA then enters TCA cycle.

Q. What are the co-enzymes required for the conversion of propionyl CoA to succinyl
CoA?
A. Biotin, ATP, Vitamin B12.

Q. Succinyl CoA is generated from which substances?

A. Odd chain fatty acids, propionic acid, valine, isoleucine, threonine.

Q. Succinyl CoA is utilised for what purposes?

A. Porphyrin biosynthesis, activation of acetoacetate, and oxidation in TCA cycle.

Q. What is alpha oxidation of fatty acid?

A. It is a process by which fatty acids are oxidized by removing carbon atoms, one at a
time, from the carboxyl end. It is used for fatty acids that have a methyl group at the
beta-carbon, which blocks beta-oxidation. Alpha oxidation does not generate energy.

Q. Where is alpha oxidation taking place?

A. In endoplasmic reticulum (microsomes).
Q. Refsum.s disease is due to what?
A. Accumulation of phytanic acid, due to defective alpha oxidation.

Q. What are the major differences between fatty acid synthesis and beta oxidation of
fatty acid?
A. Beta oxidation is taking place in mitochondria, fatty acid synthesis is in
cytoplasm. Oxidation enzymes are independent, synthetic enzymes are grouped as
a multi-enzyme complex. During oxidation, 2 carbon units are removed as acetyl CoA,
during synthesis, 2 carbon units are added as 3 carbon malonyl CoA. For oxidation,
NAD and FAD are necessary, for synthesis, NADPH is used.

Q. How NADPH is made available?

A. In the HMP shunt pathway, glucose-6-phosphate dehydrogenase reaction produces
NADPH.

Q. What is the rate limiting enzyme of de novo synthesis of fatty acid?

A. Acetyl CoA carboxylase.

Q. What is the reaction?

A. Acetyl CoA + CO2 ® Malonyl CoA.

Q. What are the co-enzymes required for the reaction?

A. Biotin and ATP.

Q. Acetyl CoA from mitochondria is transferred to cytoplasm for the de novo synthesis
of fatty acid, by which enzyme?
A. ATP citrate lyase.

Q. What are the steps in which NADPH is used in fatty acid synthesis?
A. Step 4 (Keto acyl reductase) and Step 6 (Enoyl reductase).

Q. Acetyl CoA is used for what purposes?

A. Fatty acid synthesis, oxidation in citric acid cycle for generation of energy, cholesterol
synthesis and ketone body formation.

Q. What are the sources of NADPH for fatty acid synthesis?

A. Glucose-6-phosphate dehydrogenase, malic enzyme, cytoplasmic malate
dehydrogenase.

Q. How is fatty acid synthesis regulated?

A. Key enzyme, acetyl CoA carboxylase, is stimulated by citrate and inhibited by
palmitoyl CoA.

Q. What is the action of insulin on fatty acid synthesis?

A. Insulin favours lipogenesis.
Q. How?
A. Insulin enhances the uptake of glucose by adipocytes and increases the activity
of pyruvate dehydrogenase. So, availability of acetyl CoA is increased. Insulin also
activates glucose-6-phosphate dehydrogenase, so that enough NADPH is available.
Moreover, insulin stimulates acetylCoA carboxylase, the key enzyme of fatty acid
synthesis pathway. (Table 10.3). Insulin also depresses the hormone sensitive lipase .

Q. Chain elongation of fatty acid is taking place in which site?

A. Microsomal elongation system is more active.

Q. Triacyl glycerol synthesis is enhanced by which hormone?

A. Insulin.

Q. In adipose tissue, what is the source of glycerol phosphate for triglyceride

formation?
A. From dihydroxy acetone phosphate, derived from glucose.

Q. White adipose tissue is concerned with what?

A. Energy storage.

Q. Brown adipose tissue is involved in what process?

A. Thermogenesis.

Q. What enzyme is involved in lipolysis?

A. By hormone sensitive lipase.

Q. What is its action?

A. In adipose tissue, hormone sensitive lipase hydrolyses triglyceride into fatty acid
and releases into blood.

Q. In the blood, fatty acids are transported as what form?

A. Albumin is the carrier of free fatty acid.

Q. Hormone sensitive lipase is activated by which hormones?

A. Growth hormone, corticosteroids, ACTH, adrenalin, and glucagon.

Q. Which are the lipolytic hormones?

A. Growth hormone, corticosteroids, ACTH, adrenalin, and glucagon.

Q. What is the mechanism of activation of hormone sensitive lipase?

A. A cascade through adenyl cyclase, cyclic AMP and kinase.

Q. What is the action of caffeine?

A. It inhibits phospho diesterase, increases activity of hormone sensitive lipase, and so,
prolongs the action of cyclic AMP. Thus, caffeine favours lipolysis.
Q. In diabetes mellitus, non-esterified fatty acid level in blood is increased, why?
A. Insulin inhibits hormone sensitive lipase, in diabetes, this inhibition is removed, so,
more lipolysis is taking place.

Q. What worsens fatty liver?

A. Alcohol, diabetes mellitus, excess calorie intake, hepatitis virus.

Q. What are the sources of acetyl CoA?

A. Pyruvate, fatty acids, acetoacetyl CoA, and leucine.

Q. What substances will prevent fatty liver?

A. Choline, methionine, lecithin.

Q. What are ketone bodies?

A. Aceto acetate, beta hydroxy butyric acid, and acetone.

Q. Ketone bodies are formed in which tissue?

A. Liver.

Q. Ketogenesis is taking place in which subcellular organelle?

A. Mitochondria.

Q. What is the rate-limiting-step in ketone body formation?

A. HMGCoA synthase.

Q. HMGCoA is directly converted into what substances?

A. Acetoacetate, acetyl CoA, mevalonate.

Q. Ketone body utilisation is taking place in which organs?

A. Ketolysis is taking place in extra hepatic tissues. (All other tissues, except liver).

Q. Utilisation of ketone bodies by peripheral tissues needs which enzyme?

A. Succinyl CoA dependent thiophorase.

Q. Ketosis is due to what processes?

A. Step 1: Absence of insulin leads to excessive hydrolysis of triacyl glycerol. Step 2:
So more fatty acid is available, and more acetyl CoA is produced. Step 3: But
oxidation of acetyl CoA in citric acid cycle is sluggish. The excess acetyl CoA
is diverted into ketone body formation.

Q. What test is used to identify ketone bodies in urine?

A. Rothera.s test.
Lipids-III: Cholesterol, Lipoproteins and
Cardiovascular Diseases
Q. What is the ring structure present in cholesterol?
A. Perhydro cyclo pentano phenanthrene ring.

Q. Cholesterol has how many carbon atoms?

A. It has 27 carbon atoms.

Q. What are the substances derived from cholesterol?

A. Glucocorticoids, mineralocorticoids, testosterone, estrogen, bile acids.

Q. Which food stuffs contain cholesterol?

A. Non-vegetarian food.

Q. Whether cholesterol is present in vegetable oils?

A. No.

Q. What is the rate-limiting-step in the cholesterol biosynthesis?

A. HMG CoA reductase.

Q. What is HMG CoA synthase?

A. It is the rate-limiting-enzyme in ketogenesis pathway.

Q. What is the first sterol ring formed during cholesterol biosynthesis?

A. Lanosterol.

Q. How cholesterol is excreted?

A. Through bile, partly as cholesterol itself, and partly as bile salts.

Q. What is the normal level of total plasma lipids?

A. 400-600 mg/dl.

Q. What is the normal level of total cholesterol?

A. 150-220 mg/dl.

Q. What is the normal level of triglycerides?

A. 50-200 mg/dl.

Q. How lipoproteins are estimated?

A. Either by electrophoresis or by ultracentrifugation.

Q. During electrophoresis, what is the fastest moving lipoprotein?

A. HDL (alpha lipoprotein).
Q. During electrophoresis, what is the least moving lipoprotein?
A. Chylomicron (gamma position).

Q. Maximum cholesterol content is in which lipoprotein?

A. LDL (Beta lipoprotein).

Q. Triglycerides present in chylomicrons are hydrolysed by what?

A. Lipoprotein lipase.

Q. Where is the enzyme present?

A. It is located at the endothelial layer of capillaries of adipose tissue, muscles and
heart, but not in liver.

Q. What is the main apoprotein present in chylomicron.

A. B48.

Q. What is the function of chylomicron?

A. Transport of triglycerides from intestine to adipose tissue.

Q. Highest content of triglycerides is seen in which lipoprotein?

A. Chylomicrons.

Q. Endogenous triglycerides in plasma are carried by what?

A. VLDL.

Q. What is the main apoprotein present in LDL?

A. B100, it is the ligand for LDL receptor.

Q. What is the function of LDL receptors?

A. LDL receptors are present on all cells but most abundant in hepatic cells and adrenal
cortex. LDL receptors, located in specialised regions called clathrin-coated pits.
When the apo B-100 binds to the receptor, the receptor-LDL complex is internalised
by endocytosis.

Q. What is the function of LDL?

A. Transport of cholesterol from liver to peripheral tissues.

Q. What is .bad cholesterol.?

A. LDL cholesterol.

Q. Why it is called so?

A. LDL transports cholesterol from liver to peripheral tissues, where it is deposited, and
causes atherosclerosis.
Q. What is lipoprotein(a) ?
A. It is attached to apo B-100 by a disulfide bond. It has significant homology with
plasminogen. So it interferes with plasminogen activation and impairs fibrinolysis . This
leads to unopposed intravascular thrombosis and possible myocardial infarction.

Q. What is the significance of lipoprotein (a)?

A. Lp(a) is associated with heart attacks at the age of 30 or 40 years. Indians have a
higher level of Lp(a) than Europeans.

Q. What is the normal level of lipoprotein (a) ?

A. In 40% population, there is no detectable level of Lp(a) in serum. In 20% of
population, the Lp(a) concentration in blood is more than 30 mg/dl, and these persons
are susceptible to heart attack at a younger age.

Q. What is the function of HDL?

A. Transport of cholesterol from peripheral tissues to liver.

Q. What is .good cholesterol.?

A. HDL cholesterol.

Q. Why it is called so?

A. HDL transports cholesterol from peripheral tissues to liver, and so helps in excretion
of cholesterol from the body. So HDL is anti-atherogenic.

Q. What is the main apoprotein present in HDL?

A. Apo A-1, it is the ligand for HDL receptor.

Q. What is LCAT?
A. Lecithin cholesterol acyl transferase.

Q. Where is it present?
A. LCAT present in plasma is activated by apo-A1, when LCAT binds to HDL disc.

Q. What is its importance?

A. The free cholesterol is esterified by LCAT the esterified cholesterol is then
incorporated into HDL disc, to form mature HDL. So for excretion of cholesterol, LCAT
is necessary.

Q. What is the importance of PUFA in cholesterol metabolsim?

A. PUFA present in lecithin is transferred to cholesterol by the enzyme LCAT. The
esterified cholesterol is then taken by HDL, and finally excreted through liver. So, for
excretion of cholesterol, PUFA is required. Thus, PUFA will lower the blood level
of cholesterol.

Q. Free fatty acids of plasma are bound to what?

A. Bound to serum albumin.
Q. What is the function of albumin?
A. Transport of free fatty acid from adipose tissue to peripheral tissues.

Q. Triglycerides present in adipose tissue are hydrolysed by what enzyme?

A. Hormone sensitive lipase.

Q. What are the salient features of hyperlipoproteinemia Type II-A?

A. Premature atherosclerosis elevated plasma LDL cholesterol, and prominent beta
band on electrophoresis.

Q. What is it due to?

A. Defect in LDL receptor.

Q. What is the treatment policy?

A. Low cholesterol diet, decreased intake of saturated fat, increased intake of
PUFA, bile acid binding resins.

Q. What is the normal serum cholesterol level?

A. 150-220 mg/dl.

Q. Hypercholesterolemia is seen in what conditions?

A. Diabetes mellitus, nephrotic syndrome, obstructive jaundice, hypothyroidism.

Q. How atherosclerosis started?

A. The effect is directly proportional to the LDL levels. Free radical induced oxidative
damage of LDL will accelerate this process. Oxidised LDL-cholesterol is deposited in
the subintimal regions of arteries.

Q. What tissues are affected mostly by atherosclerosis?

A. Aorta, coronary arteries and cerebral vessels are predominantly affected.

Q. How LDL deposit leads to atherosclerosis?

A. Oxidised LDL is taken up by macrophages, the macrophages become overloaded
with cholesterol esters, and these are then called .foam cells. Which form the hallmark
of atherosclerotic plaques.

Q. What happens to atherosclerotic plaque?

A. This leads to narrowing of vessel wall. Then fibrous proliferation takes place, this is
due to liberation of various growth factors. Again a clot is formed which occludes one of
the major vessels. Then there is ischemia of the tissue supplied. Finally infarction or
ischemic death of the tissue occurs.

Q. What are the important risk factors of coronary artery diseases?

A. Serum cholesterol level above 220 mg/dl, LDL-cholesterol level above 160 mg/dl,
HDL-cholesterol level below 35 mg/dl, and Apo(a) above 30 mg/dl.
Q. What are other risk factors associated with coronary artery diseases?
A. Cigarette smoking, hypertension, diabetes mellitus, serum triglyceride level above
200 mg/dl,homocysteine level, sedentary life style, obesity.

Q. What advise you will give to a person with increased cholesterol level?
A. Reduce food with higher cholesterol content of food, include PUFA and omega-3
fatty acids in diet, reduction of total fat intake of green leafy vegetables, exercise, avoid
cigarettes.

Q. When will you start drugs for a person with increased cholesterol level?
A. When patient.s condition is not responding to the dietary restriction.

Q. What are the drugs available to treat hypercholesterolemia?

A. Bile acid binding recins, HMGCoA reductase inhibitors, fibrate derivatives, nicotinic
acid.

Q. What is the function of bile acids?

A. They are the major route of excretion of cholesterol and they are required for
absorption of triacylglycerol.

Q. Bile acids are derived from what substance?

A. Cholesterol.

Q. How are bile salts formed?

A. Bile acids conjugated with taurine or glycine.

Lipids-IV: MCFA, PUFA and Prostaglandins

Q. What is MCFA?
A. Medium chain fatty acids they contain 8 to 14 carbon atoms.

Q. What is LCFA?
A. Long chain fatty acids they contain 16 to 18 carbon atoms.

Q. What is VLCFA?
A. Very long chain fatty acids they contain 20 or more carbon atoms.

Q. What is the difference in digestion of MCT from that of LCFA?

A. MCT containing triglycerides are digested by MCT-specific lipase. Pancreatic
lipase and bile salts are not required.
Q. What is the difference in absorption of MCFA from that of LCFA?
A. MCFA is absorbed directly to blood (not to lacteals, as in the case of LCFA).
Further, after absorption, MCFA is carried by albumin in blood, whereas LCFA are
absorbed as triglycerides and carried by chilomicrons.

Q. So what is the advantage of MCFA?

A. MCFA are easily digested, easily absorbed, and easily oxidised (when compared to
LCFA).

Q. When palmitoleic acid (16 C, 1 double bond) is completely oxidised, what is the net
generation of ATP molecules?
A. 127.

Q. When unsaturated fatty acids are oxidised, how many ATP is formed?
A. The energy yield is less by 2 ATP molecules per double bond, when compared to the
corresponding chain length saturated fatty acid.

Q. Why 2 ATP molecules are reduced?

A. Because, the FAD dependent dehydrogenation (step 1 of beta oxidation) does
not occur at the double bond.

Q. Name polyunsaturated fatty acids.

A. Linoleic, linolenic and arachidonic acids.

Q. What are essential fatty acids?

A. Those cannot be synthesised by the body. So they are to be provided in the diet.

Q. Name the essential fatty acids.

A. Linoleic and linolenic acids are the only fatty acids which cannot be synthesised in
the body.

Q. Where does desaturation of fatty acid takes place?

A. In the endoplasmic reticulum.

Q. What is the enzyme called?

A. Microsomal desaturase system.

Q. What are the important substances derived from PUFA?

A. Prostaglandins, prostacycline, thromboxanes, leukotienes, HPETE.

Q. What are the functions of PUFA?

A. Synthesis of prostaglandins, synthesis of phospholipids and esterification of
cholesterol.
Q. How prostaglandins are classified?
A. According to the attachment of different substituent groups to the ring, PGs are
named with capital letters such as A, B, E and F. In the same series, depending on
number of double bonds on the side chains they are denoted by a subscript after the
capital letter, e.g. PGE1, PGE2, PGE3, etc. Series 2 have two double bonds at 13-14
(trans) and 5-6 (cis). This is the most common variety.

Q. Prostaglandins are derived from what substance?

A. Prostaglandins are derived from the PUFA. The Series 2 (with two double bonds) are
derived from arachidonic acid. All naturally occurring PGs belong to the 2-series.

Q. Prostaglandins are stored in what form?

A. As precursors, as membrane phospholipids.

Q. How prostaglandins are synthesised?

A. The arachidonic acid is released by the action of phospholipase A2 on phospholipids
prostaglandin synthesis is catalysed by prostaglandin H synthase (PGHS). It contains
two separate enzyme activities, cyclo-oxygenase and peroxidase.
Q. How prostaglandin synthesis is regulated?
A. The phospholipase is activated by epinephrine. Steroids inhibit PL and prevent
release of arachidonic acid from membranes.

Q. What is the importance of cyclo-oxygenase?

A. Cyclo-oxygenase is activated by catecholamines and inhibited by non-steroid anti-
inflammatory drugs (NSAIDS). Cyclo-oxygenase is a .suicide. enzyme.

Q. What is the mechanism of action of aspirin?

A. Aspirin acetylates serine in the active site and irreversibly inhibits the cyclo-
oxygenase.

Q. How is prostaglandins inactivated?

A. Prostaglandins have only very short half life, of about 30 seconds. They are
inactivated by the 15-hydroxy-prostaglandin-dehydrogenase which converts 15-OH
group to keto group.

Q. What is the mechanism of action of prostaglandins?

A. Prostaglandins are local hormones, and function through G-protein coupled receptors
In most tissues, PGE increases cAMP level. But in adipose tissue and in renal tubular
cells, PGE lowers cAMP level.

Q. What is the action of prostacyclin on vascular endothelium?

A. Prostacyclin causes vasodilatation. It also inhibits platelet aggregation and has a
protective effect on vessel wall against deposition of platelets.
Q. What is the effect of thromboxane?
A. Thromboxane (TXA2) is the main PG produced by platelets. The major effects are
vasoconstriction and platelet aggregation. Prostacyclin and thromboxane are
opposing in activity.

Q. What is the precursor of leukotrienes?

A. They are produced from arachidonic acid.

Q. What is its biological importance?

A. LT B4 is produced in neutrophils, it is the most potent chemotactic agent. The slow
reacting substance of anaphylaxis (SRS-A) contains LTC4, LTD4 and LTE4. They
cause smooth muscle contraction, constrict the bronchioles, increase capillary
permeability and produce vasoconstriction.

Q. What are VLCFAs?

A. Fatty acids having 20 or more carbon atoms are called very long chain fatty acids
(VLCFA). Eicosapenta-enoic acid (EPA) (Timnodonic acid, C-20, 5 double bonds) and
docosa hexa-enoic acid (DHA) (cervonic acid, C-22, 6 double bonds) are good
examples of VLCFA.

Q. What is the importance of DHA?

A. DHA is synthesised linolenic acid. DHA can be obtained from fish oils or from milk.
DHA is especially required for the development of brain and retina. Low levels of
DHA in blood is seen in patients with retinitis pigmentosa.

Lipids-V: Compound Lipids

Q. How phospholipids are classified?
A. 1. Nitrogen containing glycero phosphatides, 2. Non-nitrogen containing glycero
phosphatides, 3. Plasmalogens, 4. Phospho sphingosides 5. Glycosphingolipids 6.
Sulpholipids.

Q. What is Lecithin?
A. Phosphatidyl choline.

Q. What is phosphatidic acid?

A. Phosphatidic acid is made up of one glycerol to which two fatty acid residues are
esterified to carbon atoms 1 and 2 and the 3rd hydroxyl group is esterified to a
phosphoric acid.

Q. What is Cephalin?
A. Phosphatidyl ethanol amine.
Q. What is Cardiolipin?
A. Diphosphatidyl glycerol.

Q. What is sphingomyelin?
A. All sphingolipids have the long aliphatic aminoalcohol sphingosine which is
attached to afatty acid in amide linkage to form a ceramide. A common
phosphosphingoside present abundantly in the nervous system, is sphingomyelin. It
contains choline. Sphingomyelins are the only sphingolipid that contain phosphate and
have no sugar moiety.

Q. What is a cerebroside?
A. Ceramide monohexoside.

Q. What is a globoside?
A. Ceramide oligosaccharides.

Q. What is lung surfactant?

A. It is produced by lung epithelial cells. Surfactant decreases surface tension of the
aqueous layer of lung and prevents collapse of lung alveoli.

Q. What are the constituents of surfactants?

A. Surfactants contain dipalmitoyl lecithin, phosphatidyl glycerol, cholesterol and
surfactant proteins A, B and C.

Q. What is its clinical significance?

A. Low levels of surfactant leads to respiratory distress syndrome (RDS), which is a
common cause of neonatal morbidity.

Q. Phospholipids can aggregate into what ?

A. Micelle and liposome.

Q. What is the nitrogenous base present in lecithin?

A. Choline.

Q. Cerebroside contains what?

A. Sphingosine, fatty acid, hexose.

Q. On hydrolysis of sphingomyelin, what are obtained?

A. Sphingosine, fatty acid, phosphoric acid, choline.

Q. A ganglioside on hydrolysis, will give rise to what?

A. Sphingosine, fatty acid, N-acetyl neuraminic acid.

Q. Name some lipid storage diseases.

A. Tay Sach.s disease, Niemann Pick.s disease, Gaucher.s disease.
Q. Gaucher.s disease is due to the deficiency of what?
A. Beta glucosidase.

Q. What is accumulated in Gaucher.s disease?

A. Glucocerebroside.

Q. Niemann-Pick disease is due to the deficiency of what?

A. Sphingomyelinase.

Q. What is accumulated in Niemann-Pick disease?

A. Sphingomyelin.

Q. Tay Sach.s disease is due to the deficiency of what?

A. Hexosaminidase.

Q. What is accumulated in Tay Sach.s disease?

A. Ganglioside.

Amino Acid Metabolism-I: General: Digestion,

Absorption, Transamination, Urea
Q. What is the enzyme mainly responsible for protein digestion in stomach?
A. Pepsin.

Q. What is the action of pepsin?

A. It hydrolyses peptide bonds formed by carboxyl groups of phenyl alanine, tyrosine,
tryptophan and methionine.

Q. How pepsinogen is activated?

A. Removal of N-terminal end by gastric hydrochloric acid.

Q. What are zymogens?

A. They are pro-enzymes, inactive at the time of secretion, but will be activated in the
gastro intestinal tract.

Q. How the activation is effected generally?

A. Activation is achieved by removing a small part of the precursor molecules. Selective
proteolysis produces the catalytic site.

Q. What is its biological significance?

A. Zymogens prevent autodigestion of the cells.
Q. What is its clinical significance?
A. Acute pancreatitis results when trypsinogen is activated prematurely.

Q. What are important enzymes in pancreatic juice?

A. Pancreatic juice contains the endopeptidases trypsin, chymotrypsin and elastase.

Q. How trypsinogen is activated?

A. The activation of trypsinogen is by removal of a hexapeptide from N-terminal end by
entero-kinase (enteropeptidase) present on the intestinal microvillus membranes.

Q. What is the action of trypsin?

A. It hydrolyses peptide bonds formed by carboxyl groups of arginine and lysine.

Q. How chymotrypsinogen is activated?

A. It is activated by trypsin.

Q. What is an endopeptidase?
A. It acts on peptide bonds inside the protein molecule, so that the protein becomes
successively smaller and smaller units.

Q. Give some examples of an endopeptidase.

A. Trypsin, pepsin.

Q. What are exopeptidases?

A. They act at one of the protein molecule, liberating amino acids sequentially, one at a
time.

Q. Give an example exopepdases.

A. Carboxypeptidase.

Q. What is carboxypeptidase?
A. It is secreted by cells of intestinal villi, it is a metallo-enzyme containing zinc, it
is an endopeptidase, spliting off carboxy terminal bond of the protein.

Q. What is required for absorption of amino acids?

A. It needs the help of glutathione.

Q. What are cathepsins?

A. Intracellular proteases.

Q. What is ubiquitin?
A. It is necessary for intracellular protein breakdown.

Q. What are proteosomes?

A. Ubiquitin tagged proteins are degraded inside the cells, with the help of proteosomes.
Q. In fasting state, nitrogen is transported from muscle as what form?
A. In the fasting state, the muscle releases mainly alanine and glutamine of which
alanine is taken up by liver and glutamine by kidneys.

Q. Transamination of glutamic acid produces what?

A. Alpha keto glutaric acid.

Q. What is the co-enzyme necessary for transamination reaction?

A. Pyridoxal phosphate.

Q. What are the physiological significance of transamination?

A. It synthesises non-essential amino acids, it helps in the equalisation of quantities of
amino acids, it is the first step of amino acid breaking down pathways.

Q. What is the clinical significance of transamination?

A. Transaminases are increased in blood in liver and cardiac diseases.

Q. What is transdeamination?
A. Transamination takes place in all the cells of the body, the amino group is
transported to liver as glutamic acid which is finally oxidatively deaminated in liver.
Thus, the two components of the reaction are physically far away, but physiologically
they are coupled. Hence the term transdeamination.

Q. Transamination reaction of pyruvate with glutamate results in the production of

what substances?
A. Alanine and alpha keto glutarate.

Q. Which amino acid is oxidatively deaminated in liver?

A. Glutamic acid.

Q. What is the reaction catalysed by glutamate dehydrogenase?

A. Glutamate alpha keto glutarate + ammonia.

Q. What is the co-enzyme required for glutamate dehydrogenase?

A. NAD.

Q. Nitrogen atoms in the urea is derived from what precursors?

A. One from ammonia and another from aspartic acid.

Q. Ammonia is immediately trapped in brain by what?

A. Glutamine synthetase.

Q. What is the reaction catalysed by glutamine synthetase?

A. Glutamic acid + ammonia ® glutamine, this requires hydrolysis of ATP to ADP.
Q. What is the key enzyme of urea synthesis?
A. Carbamoyl phosphate synthetase.

Q. What are the two carbamoyl phosphate synthetases?

A. CPS-I is involved in urea synthesis, CPS-II is required for pyrimidine synthesis. CPS
is seen in mitochondria, while CPS-II is in cytosol.

Q. What is the normal blood urea level?

A. 20-40 mg/dl.

Q. Blood urea level is markedly increased in which condition?

A. Renal diseases.

Q. What is the normal urinary excretion of urea?

A. 15-30 mg/day.

Amino Acid Metabolism-II:Simple, Hydroxy and

Sulfur Containing Amino Acids Glycine, Serine,
Alanine, Threonine, Methionine, Cysteine
Q. Glycine is used for synthesis of what compounds?
A. Serine, Creatine, Purines, Heme, Glutathione, Bile salts.

Q. For creatine synthesis, which amino acids are used?

A. Glycine, arginine, methionine.

Q. Guanido acetic acid is formed in which tissue?

A. Kidney.

Q. Guanido acetic acid is formed from what amino acids?

A. Arginine + glycine.

Q. Where is creatine is synthesised?

A. In liver.

Q. What is the significance of creatinine?

A. Excretion is increased in muscle dystrophy.

Q. How creatinine is produced in the body?

A. By spontaneous degradation of creatine phosphate.

Q. What are the sources of oxalic acid in urine?

A. Ascorbic acid and glycine.
Q. What is the cause of hyper oxaluria?
A. Protein targeting defect.

Q. What are the important substances produced from serine?

A. Glycine, pyruvate,cysteine,selenocysteine, choline, phosphatidyl serine.

Q. On decarboxylation, serine will produce what?

A. Ethanol amine.

Q. Choline is derived from what?

A. Serine.

Q. What is the product of transamination of alanine?

A. Pyruvic acid.

Q. What is the significance of glucose-alanine cycle?

A. During starvation, alanine is released from muscle, and is taken up by liver. In liver
alanine is transaminated to pyruvate, and pyruvate undergoes gluconeogenesis.

Q. What are important substrates for transmethylation reactions?

A. Guanido acetic acid, serine, nor-epinephrine, N-acetyl serotonin.

Q. What is the methyl donor in transmethylation reaction?

A. S-adenosyl methionine.

Q. Which amino acid has two optically active (asymmetric) carbon atom?
A. Threonine.

Q. What are the functions of glutathione?

A. Reduction of met-hemoglobin to hemoglobin, keeping RBC membrane integrity,
carrying amino acids across membranes, and detoxification of peroxidases.

Q. What is glutathione?
A. Gamma glutamyl cysteinyl glycine.

Q. Urine of a patient with homocystinuria will be positive for which test?

A. Cyanide nitroprusside test.

Q. What is the defective enzyme in homocystinuria?

A. Cystathionine synthase.

Q. What are the characteristic features of homocystinuria?

A. Mental retardation, subluxation of lens, and thrombosis.

Q. Homocystinuria is due to abnormal metabolism of which amino acid?

A. Methionine.
Q. What is the defective enzyme in Cystathionuria?
A. Cystathionase.

Amino Acid Metabolism-III:Acidic, Basic and

Branched Chain Amino Acids, Glutamic acid,
Glutamine, Aspartic acid, Asparagine, Lysine, Nitric
Oxide, Valine, Leucine, Isoleucine
Q. What are the major functions of glutamic acid?
A. Transamination, transdeamination, ammonia trapping in brain, and production of
gamma amino butyric acid.

Q. Transamination reaction of pyruvate with glutamate results in the production of

what substances?
A. Alanine and alpha keto glutarate.

Q. Which amino acid is oxidatively deaminated in liver?

A. Glutamic acid.

Q. What is the reaction catalysed by glutamate dehydrogenase?

A. Glutamate ® alpha keto glutarate + ammonia.

Q. What is the co-enzyme required for glutamate dehydrogenase?

A. NAD.

Q. Ammonia is immediately trapped in brain by what?

A. Glutamine synthetase.

Q. What is the reaction catalysed by glutamine synthetase?

A. Glutamic acid + ammonia ® glutamine, this requires hydrolysis of ATP to ADP.

Q. What is the reaction catalysed by glutaminase?

A. Glutamine ® glutamic acid + ammonia.

Q. Glutaminase enzyme is used for what purpose?

A. Excretion of ammonia in kidney tubules.

Q. Transamination of glutamic acid will give rise to what?

A. Alpha keto glutarate.
Q. Decarboxylation of glutamic acid will give rise to what?
A. Gamma amino butyric acid.

Q. What is GABA?
A. It is an inhibitory neurotransmitter. Which is produced by decarboxylation of glutamic
acid.

Q. Which will give rise to an inhibitory neurotransmitter?

A. Glutamic acid.

Q. Glutamic acid can be formed from which amino acids?

A. Histidine, arginine, proline, glutamine.

Q. Transamination of pyruvic acid will give rise to what?

A. Alanine.

Q. Transamination of oxaloacetic acid will give rise to what?

A. Aspartic acid.

Q. What are the functions of glutamine?

A. Ammonia trapping in brain (glutamic acid + ammonia to glutamine), ammonia
production in kidney (glutamine to glutamic acid + ammonia), synthesis of purine
(Nitrogen 3 and 9), synthesis of pyrimidine (3rd Nitrogen), synthesis of guanine and
cytosine (amino groups).

Q. Alpha amino group of aspartic acid is incorporated into which compounds?

A. Purines (1st nitrogen and 6th amino), pyrimidines (1st nitrogen and C4,5,6), and
urea.

Q. Which amino acids are required for both purine and pyrimidine synthesis?
A. Aspartic acid, glutamine.

Q. What is asparaginase?
A. Enzyme catalysing the reaction asparaginase to aspartic acid + ammonia.

Q. What is its function?

A. Ammonia production in kidney tubules.

Q. What is its clinical application?

A. It is an anticancer drug against leukemias and lymphomas. The leukemia cells
cannot synthesis glutamine, and the available glutamine is destroyed by
glutaminase, leukemia cells will starve and die.

Q. Lysine is deficient in which food stuffs?

A. Lysine is deficient in cereals.
Q. Carnitine is synthesised from which amino acid?
A. Lysine.

Q. Nitric oxide synthase system needs which coenzymes?

A. FAD, FMN, tetra hydro biopterine, NADPH.

Q. What are the iso-enzymes of nitric oxide synthase?

A. Neuronal NOS, inducible NOS (macrophages) and endothelial NOS.

Q. What are the major functions of nitric oxide?

A. Vasodilatation, keeping the normal blood pressure, inhibitioin of adhesion of
platelets, memory process in brain, bactericidal in macrophages.

Q. What is the precursor of nitric oxide?

A. Arginine.

Q. Which will give rise to polyamines?

A. Ornithine.

Q. What are polyamines?

A. Polyamines are putrescine, spermine and spermidine.

Q. What are the functions of polyamines?

A. They are growth factors, their concentration is increased in cancer.

Q. Name some mono amines.

A. Histamine, dopamine, and serotonin.

Q. What about glutamine? Is it an amine?

A. No. Glutamine is an amide of glutamic acid.

Q. Valine enters in which metabolism?

A. Valine is glucogenic.

Q. Leucine enters in which metabolism?

A. Leucine is ketogenic.

Q. Isoleucine joins in which metabolism?

A. Isoleucine is partly glucogenic and partly ketogenic.

Q. Branched chain keto acids are excreted in urine n what condition?

A. Maple syrup urine disease.

Q. What is the defect in maple syrup urine disease?

A. Deficient decarboxylation of branched chain ketoacids.
Amino Acid Metabolism-IV: Aromatic Amino
Acids: Phenyl alanine, Tyrosine, Tryptophan, Histidine
Q. Which amino acids are both glucogenic and ketogenic?
A. Phenyl alanine, tyrosine, tryptophan, and isoleucine.

Q. What are the important substances synthesized from tyrosine?

A. Melanin, thyroxine, epinephrine and norepinephrine.

Q. What is the immediate precursor of norepinephrine?

A. Dopamine.

Q. In pheochromocytoma, urine contains what substance?

A. Vanillyl mandelic acid.

Q. Phenyl alanine level in blood is increased in what condition?

A. Phenyl ketonuria.

Q. What is the defective enzyme in phenyl ketonuria?

A. Phenyl alanine hydroxylase.

Q. What are the co-enzymes required for phenylalanine hydroxylase?

A. NADH, NADPH, tetrahydro bioptrin.

Q. Phenyl alanine, on transamination will give rise to what?

A. Phenyl pyruvate.

Q. What are the salient features of phenylketonuria?

A. Mental retardation, hyperactivity, high blood phenyl alanine.

Q. Phenyl pyruvic acid is excreted in urine in which condition?

A. Phenyl ketonuria.

Q. Homogentisic acid is excreted in urine in which condition?

A. Alkaptonuria.

Q. What is the defective enzyme in alkaptonuria?

A. Homogentisic acid oxidase.

Q. Ochronosis is a manifestation of which condition?

A. Alkaptonuria.

Q. What is associated manifestation of albinism?

A. Nystagmus.
Q. A person.s urine was found to turn black on standing and gave a positive
Benedict.s test. He is likely to have what condition?
A. Alkaptonuria.

Q. In phenyl ketonuria, urine will be positive for what test?

A. Ferric chloride test.

Q. What is the defect in tyrosinemia type I (hepatorenal tyrosinemia)?

A. Fumaryl acetoacetate hydrolase deficiency.

Q. What is the defect in tyrosinemia type II (oculocutaneous tyrosinemia?

A. Deficiency of tyrosine amino transferase.

Q. Tryptophan is deficient in which food stuff?

A. Maize and corn.

Q. Xanthurenic acid in urine is seen in which condition?

A. Pyridoxal deficiency.

Q. What are the important substances produced from tryptophan?

A. Serotonin, melatonin, niacin, alanine, and acetoacetate.

Q. Which amino acid will give rise to a vitamin?

A. Tryptophan.

Q. Serotonin is derived from which amino acid?

A. Tryptophan.

Q. What are the characteristic features of malignantcarcinoid syndrome

(argentaffinoma)?
A. Niacin deficiency, increased serotonin production, increased hydroxy indole acetic
acid excretion, fluctuating hypertension.

Q. Pellagra is manifested in which conditions?

A. Niacin deficiency, pyridoxal deficiency, tryptophan deficiency, and carcinoid
syndrome.

Q. What is Hartnup.s disease?

A. Absorption of aromatic amino acids from intestine as well as reabsorption from
renal tubules are defective. So tryptophan deficiency, and pellagra ike symptoms are
seen.

Q. Tryptophan is excreted in large quantities in which condition?

A. Hartnup.s disease.
Q. In Hartnup.s disease, which test will give a positive test?
A. Obermeyer test will be positive in urine.

Q. Indican in urine is tested by what method?

A. Obermeyer test.

Q. What is indican?
A. Putrefaction product of tryptophan.

Q. What is the amino acid which has maximum buffering capacity at physiological
pH?
A. Histidine.

Q. What is the decarboxylation product of histidine?

A. Histamine.

Q. Which is the vasodialator produced from histidine?

A. Histamine.

Q. What is the clinical significance of histamine?

A. It is a powerful vasodilator and mediator of anaphylaxis.

Q. What is Figlu excretion test?

A. In folic acid deficiency, there is a block in histidine metabolism, and figlu is
excreted in large quantities in urine.

Q. What is figlu?
A. Formimino glutamic acid, it is a product of histidine metabolism.

Amino Acid Metabolism-V: Inter-relations of

amino acid metabolisms, One carbon metabolism,
Amino acidurias
Q. Tetra hydro folic acid is used for what purpose?
A. It is the carrier of one carbon compounds.

Q. Name one carbon compounds?

A. Formyl, formimino, methenyl, hydroxymethyl, methylene, and methyl.

Q. Which are the donors to one carbon pool?

A. Serine, choline, glycine, tryptophan, histidine.
Q. One carbon units are used for synthesis of what?
A. C2 of purine, C8 of purine, serine, dTMP, choline, creatine, epinephrine.

Q. Which is the purely ketogenic amino acid?

A. Leucine.

Q. What are partially ketogenic and partially glucogenic amino acids?

A. Phenyl alanine, tyrosine, tryptophan, isoleucine.

Q. What are important aminoacidurias which cause mental retardation?

A. Phenyl ketonuria, homocystinuria, maple syrup urine disease.

Q. What is the defect in phenylketonuria?

A. Deficiency of phenyl alanine hydroxylase.

Q. What is the defect in alkaptonuria?

A. Deficiency of homogentisic acid oxidase.

Q. What is the defect in homocystinuria (type 1)?

A. Deficiency of cystathionine beta synthase.

Q. What is the defect in maple syrup urine disease?

A. Deficiency of branched chain keto acid decarboxylase.

Q. What is the defect in cystathionuria?

A. Deficiency of cystathionase.

Q. What are the steps in which carbon dioxide is liberated, during the oxidation of
glucose?
A. Pyruvate dehydrogenase, isocitrate dehydrogenase, alpha keto glutarate
dehydrogenase.

Q. Acetyl CoA is produced from what substrates?

A. Pyruvate, fatty acids, and leucine.

Q. Acetyl CoA is used for what purposes?

A. Oxidation in TCA cycle, fatty acid synthesis, cholesterol synthesis, and ketone
body formation.

Q. Give examples of substrate level phosphorylation.

A. 1,3-bisphospho glycerate kinase, pyruvate kinase, and succinate thiokinase.
Citric Acid Cycle
Q. Which is the substrate level phosphorylation step in the TCA cycle?
A. Succinate thiokinase.

Q. What is the inhibitor of succinate dehydrogenase?

A. Malonate.

Q. Give examples of reactions in which NADH is generated.

A. Pyruvate dehydrogenase, isocitrate dehydrogenase, and alpha keto glutarate
dehydrogenase.

Q. How many ATPs are generated per one rotation of the citric acid cycle?
A. 12 ATP.

Q. What is the net yield of ATP from one molecule of glucose in anaerobic glycolysis?
A. 2 ATP.

Q. What is the net yield of ATP from one molecule of glucose in aerobic glycolysis?
A. 8 ATP.

Q. During complete oxidation, what is the net yield of ATP from one glucose molecule?
A. 38 ATP.

Q. Which is the amphibolic pathway?

A. Citric acid cycle.

Q. How TCA cycle is regulated?

A. Availability of ATP, NAD+ and oxaloacetate.

Q. Succinyl CoA is formed from which substrates?

A. Isoleucine, valine, methionine, andodd chain fatty acids.

Q. Fumarate is produced from which substances?

A. A. Arginino succinate B. Phenyl alanine.

Q. Alpha keto glutaric acid is formed from which substances?

A. Glutamic acid, histidine, arginine, and proline.

Q. Aspartic acid enters the TCA cycle at which level?

A. Oxalo acetate.
Q. In normal resting state, most of the glucose is utilised by which tissue?
A. Brain.

Q. What is the approximate percentage of storage form of energy (total fuel reserve)
present in a normal human body?
A. Fat 85%, glycogen 1%, protein 14%.

Q. During starvation, which substances are increased in blood?

A. Ketone bodies, glucagon, and epinephrine.

Electron Transport Chain

Q. Give examples of high energy compounds.
A. ATP, GTP, creatine phosphate, 1,3-bis phosphor glycerate, phosphoenol pyruvate,
acetyl CoA, and succinyl CoA.

Q. On hydrolysis of 1 mole of ATP to ADP, the release of energy will be approximately

how much?
A. 7 kCal.

Q. Where is respiratory chain located?

A. In the inner mitochondrial membrane.

Q. How is respiratory chain organised?

A. Components are organised into four complexes.

Q. What are the activities taking place inside mitochondria?

A. Citric acid cycle, electron transport chain, and beta oxidation fatty acid.

Q. Where are enzymes of citric acid cycle located?

A. Fluid matrix contains enzymes of citric acid cycle.

Q. What is the function of Co-enzyme Q?

A. It catalyses the electron transport from complex I or II to complex III.

Q. Cytochrome oxidase is present in which complex?

A. Complex IV.

Q. What are NAD+ linked dehydrogenases?

A. Glyceraldehyde-3-phosphate dehydrogenase, pyruvate dehydrogenase, alpha
keto glutarate dehydrogenase, isocitrate dehydrogenase, malate dehydrogenase, beta
hydroxy acyl CoA dehydrogenase.
Q. What are FAD-linked dehydrogenases?
A. Succinate dehydrogenase, and acyl CoA dehydrogenase.

Q. Which cytochromes contain copper?

A. Cytochrome oxidase.

Q. What is valinomycin?
A. It acts as an ionophore, dissipates the proton gradient, and so inhibits ATP
synthesis.

Q. What is atractylocide?
A. It inhibits translocase, and inhibits ATP synthesis.

Q. What are the salient features of ATP synthase?

A. It has two subunits, Fo is a proton channel, and F1 has catalytic activity.

Q. How many ATP are produced in the oxidation of one molecule of NADH?
A. Three.

Q. How many ATP are produced in the oxidation of one molecule of FADH?
A. Two.

Q. Which is complex V of respiratory chain?

A. ATP synthase.

Q. What is oligomycin?
A. It inhibits oxidative phosphorylation.

Q. Name some inhibitors of oxidative phosphorylation.

A. Oligomycin, carbon monoxide, and cyanide.

Q. Which inhibits electron transport chain at site 1?

A. Barbiturate.

Q. Which inhibits electron transport chain at site 2?

A. Naphthoquinone.

Q. Which inhibits electron transport chain at site 3?

A. Carbon monoxide and cyanide.

Q. What is the cause for death due to cyanide poisoning?

A. Cyanide inhibits cytochrome oxidase.

Q. Which is a physiological uncoupler?

A. Thyroxine.
Q. Which is the inborn error due to a mutation in NADH-Q reductase?
A. Leber.s hereditary neuropathy (LHON).

Free Radicals and Anti-oxidants

Q. Name the free radicals.
A. Superoxide anion radical, hydroperoxyl radical, hydrogen peroxide, hydroxyl
radical, lipid peroxide radical, singlet oxygen, nitric oxide, and peroxy nitrite.

Q. What are the important characteristics of reactive oxygen species?

A. Extreme reactivity, short life span, generation of new ROS by chain reaction, and
damage to various tissues.

Q. What are the enzymes generating ROS in macrophages?

A. NADPH oxidase, superoxide dismutase, and myeloperoxidase.

Q. What are the biological effects of ROS?

A. Protein damage, loss of function, lipid peroxidation, membrane damage,
mitochondrial damage, DNA damage, cell death, mutation, and cancer.

Q. What are the free radical scavinging enzymes?

A. Superoxide dismutase, glutathione peroxidase, glutathione reductase, and
catalase.

Q. ROS causes what diseases?

A. Chronic inflammation, rheumatoid arthritis, acute inflammations, bronchopulmonary
dysplasia, respiratory distress syndrome, retrolental fibroplasia, cataract, reperfusion
injury, atherosclerosis, and peptic ulcer.

Q. Name important anti-oxidants.

A. Alpha tocopherol (Vitamin E), Vitamin C, Vitamin A, and beta carotene.

Q. What is normal serum albumin level?

A. 3.5-5 mg/dl.

Q. What is the normal value of total proteins in serum?

A. 6-8 g/100 ml.

Q. Edema due to hypoproteinemia is seen in which conditions?

A. Cirrhosis liver, malnutrition, and nephritic syndrome.

Q. In blood, albumin carries what substances?

A. Free fatty acids, bilirubin, salicylate, and calcium.
Q. What is the clinical application of albumin carrying bilirubin?
A. Bilirubin and salicylate compete for binding to albumin, and so it is not safe to
give salicylate to infants having hemolytic disease.

Plasma Proteins
Q. What are the functions of albumin?
A. It maintains colloidal osmotic pressure of plasma, and it transports non-esterified
fatty acid and bilirubin.

Q. Albumin is synthesised in which organ?

A. Liver.

Q. Where is gamma globulins synthesised?

A. By reticulo endothelial system (Spleen, lymph nodes).

Q. Polymorphism is exhibited by which proteins?

A. Haptoglobin, transferrin, and ceruloplasmin.

Q. Albumin globulin ratio is reversed in which conditions?

A. Cirrhosis, chronic infections, nephrotic syndrome, and multiple myeloma.

Q. Name some transport proteins.

A. Transthyretin (thyroid hormones), retinol binding protein, thyroxine binding globulin,
transcortin (cortisol), haptoglobin (hemoglobin), transferring (Iron), and hemopexin (free
heme).

Q. Name acute phase proteins.

A. C-reactive protein, ceruloplasmin, and haptoglobin.

Q. What is the clinical manifestation of Alpha-1-anti-trypsin deficiency?

A. Emphysema and chronic lung infections.

Q. What is ceruloplasmin?
A. It is a copper containing enzyme (ferroxidase) seen in blood. It is an acute phase
protein.

Q. What is the clinical significance of ceruloplasmin?

A. Ceruloplasmin level in blood is decreased in Wilson.s hepatolenticular
degeneration.

Q. What is the carrier protein of copper?

A. Albumin.
Q. Hemopexin carries what?
A. Free heme.

Q. How hemophilia is manifested?

A. Non-stopping hemorrhage after minor injuries.

Q. How hemophilia is transmitted?

A. It is inherited as an x-linked recessive trait, males are affected, females are carriers.

Q. Hemorrhage tendency is seen in which conditions?

A. Hemophilia, Vitamin K deficiency, and thrombocytopenia

Immunochemistry
Q. How immunoglobulins are classified?
A. IgG, IgM, IgA, IgD and IgE.

Q. What is the basic structure of an immunoglobulin?

A. Two heavy chains and two light chains connected by disulphide linkages.

Q. The antigen binding capacity of immunoglobulin resides at which region of

immunoglobulin?
A. Variable region.

Q. What is primary response antibody?

A. Immunoglobulin M.

Q. What is the secondary response antibody?

A. Immunoglobulin G.

Q. Which antibody is seen in body secretions?

A. Immunoglobulin A.

Q. What is the clinical importance of immunoglobulin E?

A. They mediate anaphylactic reaction.

Q. What is the cause of anaphylactic reaction?

A. IgE attach on mast cells, when antigen is introduced, antigen antibody reaction
occurs, and leading to mast cell degranulation.

Q. What is M band?
A. A narrow peak in gamma globulin, caused by monoclonal antibodies secreted
by malignant plasma cells.
Q. What is Bence Jones protein?
A. It is the light chains of immunoglobulins, excreted in urine. It is seen in urine of 20%
cases of multiple myeloma.
Q. What is the test done to detect Bence Jones protein?
A. It is precipitated when heated between 45 and 60 degrees.

Q. How antibody diversity is produced?

A. By somatic recombination.

Q. What is the structural arrangement of collagen?

A. It has triple stranded quarter staggered arrangement. One-third residues are
glycine. About 1% residues are proline and hydroxyl proline.

Q. What are the post-translational modifications taking place in collagen?

A. Hydroxylation of proline and lysine residues, and hydrolysis of pro-collagen.

Q. Hydroxylation of proline and lysine needs what?

A. It depends on vitamin C.

Q. In ascorbic acid deficiency, what happens?

A. Poor hydroxylation, defective collagen and scurvy.

Specialised Proteins: Collagen, Myosin

Q. Cross links in collagen are formed by what?
A. It is formed between lysine and hydroxy lysine residues. It is called desmosine.

Q. What is the enzyme for cross linkage formation?

A. Lysyl oxidase.

Q. What is its clinical application?

A. Lysyl oxidase contains copper. So, in copper deficiency lysine cross-link
formation is deficient, leading to defective collagen.

Q. What are inherited disorders leading to defective collagen formation?

A. Osteogenesis imperfecta, Ehlers-Danlos syndrome, dermatoparaxis,
homocystinuria, and marfan.s syndrome.

Q. What is myosin?
A. It is a specialised protein seen in muscle.

Q. What is its biological function?

A. It can bind actin to form actomyosin. It has ATPase activity.
Q. What is the function of Troponin-C ?
A. It binds calcium.

Q. What is the function of Troponin-I ?

A. ATPase inhibitory element.

Q. What is the clinical significance of Troponin-T ?

A. Its serum level is increased in myocardial infarction.

Q. What is the chemical structure of heme?

A. It is ferro protoporphyrin.

Q. What are the substituent groups of heme?

A. Methyl, vinyl, and propionyl groups.

Q. Heme is synthesised from what substances?

A. It is synthesised from glycine and succinyl CoA.

Q. What is the rate limiting enzyme of heme synthesis?

A. ALA synthase.

Q. Which enzyme is inhibited by lead?

A. ALA dehydratase and ferrochelatase.

Q. Methenyl bridge of protoporphyrin is derived from what?

A. Alpha carbon of glycine.

Heme Synthesis and Breakdown

Q. How is heme synthesis regulated?
A. ALA synthase is repressed by heme, and ALA synthase is allosterically inhibited
by hematin.

Q. What is the action of barbiturates on heme synthesis?

A. Barbiturates will induce heme synthesis.

Q. What is the treatment for acute intermittent porphyria?

A. High carbohydrate diet, and stoppage of barbiturates.

Q. What is the defect in acute intermittent porphyria?

A. PBG-deaminase.

Q. How porphyrins are detected?

A. They show fluorescence under ultra violet light.
Q. In acute intermittent porphyria, urine contains what?
A. ALA and PBG.
Q. Lead poisoning results in elevated levels of what?
A. Delta amino levulinic acid.

Q. Degradation of heme needs which enzyme?

A. Heme oxygenase system, with NADPH.

Q. Degradation of heme to bilirubin releases what gas?

A. Carbon monoxide.

Q. Heme is converted to bilirubin in which site?

A. Microsomes of reticulo-endothelial cells.

Q. Bilirubin in blood is carried by what?

A. Albumin.

Q. How it is made water soluble?

A. By conjugation with glucuronic acid.

Q. Where is the conjugation taking place?

A. In liver.

Q. What is the enzyme?

A. UDP-glucuronyl transferase.

Q. What is the normal level of plasma bilirubin?

A. 0.2-0.8 mg/dl.

Q. What is the normal level of conjugated bilirubin in plasma?

A. Less than 0.2 mg /dl.

Q. What is latent jaundice?

A. When plasma bilirubin is between 1 to 2 mg/dl.

Q. What is jaundice?
A. When plasma bilirubin is more than 2 mg/dl, it diffuses into tissues, causing yellowish
discolouration of tissues.

Q. Enterohepatic circulation is seen in which substances?

A. Urobilinogen and bile salts.

Q. What is the defect in Gilbert.s disease?

A. Uptake of bilirubin by the liver is defective.
Q. What is the defect in Criggler-Najjar syndrome?
A. Defect in conjugation of bilirubin due to deficiency of UDP glucuronyl transferase.

Q. Conjugated hyperbilirubinemia is seen in which condition?

A. Dubin Johnson.s syndrome.

Q. Bilirubin in serum is estimated by what test?

A. Van den Bergh reaction.

Q. What is Direct van den Bergh.s reaction?

A. The colour is developed immediately when blood is added.

Q. What is your inference, when direct test is positive?

A. Blood contains conjugated bilirubin, it is water soluble.

Q. What is indirect van den Bergh.s test?

A. When blood is added to the solution, there is no colour, but when alcohol is
added, colour is developed.

Q. What is the reason for this type of reaction?

A. Bilirubin is soluble in alcohol, and alcohol extract gives the reaction.

Q. What is kernicterus?
A. In young children, when plasma bilirubin is more than 20 mg/dl, it diffuses into
brain, causing permanent damage to brain cells.

Q. In obstructive jaundice, what is seen in blood?

A. Conjugated bilirubin in excess quantity.

Q. Bile salts and bile pigments are excreted in urine in which condition?
A. Obstructive jaundice.

Q. Increased urobilinogen in urine is seen in which conditions?

A. Congenital spherocytosis, mismatched transfusion, Rh incompatibility, auto-
immune hemolysis, and glucose-6-phosphate dehydrogenase deficiency.

Haemoglobins
Q. What are the salient structural features of hemoglobin molecule?
A. Hb has four subunits, two alpha and two beta units. It contains four iron atoms.

Q. How many molecules of oxygen can bind with hemoglobin?

A. Hb can bind four molecules of oxygen.
Q. 100 ml of blood can carry how much oxygen?
A. 20 ml.

Q. What is Bohr effect?

A. The influence of pH and pCO2 to facilitate oxygenation of Hb in the lungs
and deoxygenation at the tissues is known as the Bohr effect.

Q. What is chloride shift?

A. When CO2 is taken up, chloride ions from the plasma would enter. This is called
chloride shift or Hamburger effect.

Q. Hemoglobin carries how much CO2?

A. Seventy five percent as isohydric transport and 15% as carbamino hemoglobin.

Q. What are the forms in which carbon dioxide is transported?

A. Dissolved form, isohydric transport, and carbamino hemoglobin.

Q. What is isohydric transport of carbon dioxide?

A. There is minimum change in pH during the transport.

Q. How this is effected?

A. The H+ ions are buffered by the deoxy-Hb.

Q. Which will decrease the affinity of hemoglobin for oxygen?

A. 2,3-BPG level.

Q. What is the structural difference between HbA and HbF?

A. HbA has two alpha and two beta chains, but HbF has two alpha and two gamma
chains.

Q. What are the laboratory tests to identify HbF?

A. HbF moves slower than HbA on electrophoresis, HbF is alkali resistant.

Q. What is the physiological significance of HbF?

A. Oxygen affinity is more for HbF than HbA. HbF is seen in foetal circulation.

Q. What is the clinical significance of HbF?

A. It is seen in adults in hemoglobinopathies and thalassemias.

Q. Why carbon monoxide becomes a poison?

A. Hb has more affinity to carbon monoxide than oxygen.

Q. What is the treatment for carbon monoxide poison?

A. Hyperbaric oxygen.
Q. Met-hemoglobin is found in which conditions?
A. Ingestion of nitrites, presence of HbM, GPD deficiency.

Q. What is met-hemoglobin?
A. Hemoglobin in which iron is in ferric state.

Q. What is the defect of met-hemoglobin?

A. It cannot release oxygen in tissues.

Q. What is the reagent used for colourimetric estimation of hemoglobin?

A. Drabkin.s reagent, to convert Hb to cyanmethemoglobin.

Q. What is hemoglobin S?
A. The glutamic acid in the 6th position of beta chain of HbA is changed to valine in
HbS.

Q. What is the cause for sickle cell anemia?

A. Solubility of deoxy HbS is lower than deoxy HbA, so HbS is precipitated
intracellularly, leading to sickle shape of RBC.

Q. How HbS is identified?

A. HbS is slower moving on electrophoresis than HbA.

Q. What is sickle cell trait?

A. Heterozygous (AS) condition, one allele is normal, the other is abnormal, so
half of Hb molecules are normal, and half abnormal.

Q. What is its clinical significance?

A. Sickle cell trait persons will not have any disease manifestations, usually. But, at
higher altitudes, hypoxia may cause manifestation of the disease. Chronic lung
disorders may also produce hypoxia-induced sickling in HbS trait.

Vitamin-I: Fat Soluble Vitamins: A, D, E and K

Q. What is the pro-Vitamin for Vitamin A?
A. Beta carotene present in plants.

Q. What is the major function of Vitamin A?

A. In vision, as the Wald.s visual cycle.

Q. What causes the nerve impulse in retina?

A. Photo-isomerisation of 11-cis retinal to all transretinal.
Q. How is all trans-retinal regenerated?
A. Trans-retinal is taken to liver, where it is made to trans-retinol, then isomerised to
cis-retinol and then to cis retinal.
Q. What are the enzymes required for this regeneration?
A. Alcohol dehydrogenase and retinol isomerase.

Q. What are other minor biological roles of Vitamin A?

A. Normal maintenance of epithelium and skin, glycoprotein synthesis,
reproduction, cell differentiation, and anti-oxidant role.

Q. What are the sources of Vitamin A?

A. Carrot, mangoes, papaya, green leafy vegetables, and fish liver oil.

Q. What are the deficiency manifestations of Vitamin A?

A. Night blindness, xerophthalmia, keratomalacia, and keratinisation of epithelium.

Q. Nyctalopia is due to the deficiency of which Vitamin?

A. Vitamin A.

Q. What is the daily requirement of Vitamin A?

A. 750 to 1000 microgram.

Q. How cholecalciferol is synthesised?

A. From 7-dehydro cholesterol in the malpighian layer of epidermis, by the action of
ultra violet rays.

Q. How Vitamin D is activated?

A. Cholecalciferol from skin reaches liver. There it is hydroxylated to form 25-hydroxy
cholecalciferol (25-HCC). It then reaches kidney, where further hydroxylation takes
place to form 1,25-dihydroxy cholecalciferol (DHCC).

Q. What is calcitriol?
A. 1,25-dihydroxy cholecalciferol, or active Vitamin D, contains three hydroxyl groups at
1, 3 and 25 positions. So it is called calcitriol.

Q. Which Vitamin acts as a pro-hormone?

A. Vitamin D.

Q. What is the function of Vitamin D?

A. It increases absorption of calcium from intestine, and it also increases mineralisation
of bone.
Q. How Vitamin D increases absorption of calcium?
A. Calcitriol binds to a cytoplasmic receptor. The hormone-receptor complex
interacts with DNA and causes transcription of specific genes that code for
calbindin. Due to the increased availability of calcium binding protein, the
absorption of calcium is increased.

Q. How is Vitamin D deficiency manifested?

A. Rickets in children and osteomalacia in adults.

Q. In renal disease, oral doses of Vitamin D may not be effective, why?

A. Hydroxylation and activation of Vitamin is taking place in kidney.

Q. What are the causes of rickets?

A. Chronic renal failure, liver diseases, and under exposure to sunlight.

Q. What is the daily requirement of Vitamin D?

A. 5-10 microgram.

Q. What is the chemical nature of Vitamin E?

A. Alpha tocopherol.

Q. What is the function of Vitamin E ?

A. Anti-oxidant.

Q. What is the relationship of selenium with Vitamin E?

A. They act synergistically as anti-oxidants.

Q. What is the source of Vitamin E?

A. Vegetable oils are rich sources of Vitamin E, e.g. wheat germ oil, sunflower oil,
safflower oil, cotton seed oil, and palm oil.

Q. What is the normal daily requirement of Vitamin E?

A. 15 mg or 33 international units.

Q. What is the chemical nature of Vitamin K?

A. Naphthoquinone derivative.

Q. What is menadione?
A. It is synthetic water soluble Vitamin K, widely used in clinical practice.

Q. What is the function of Vitamin K?

A. Gamma carboxylation of clotting factors such as prothrombin.

Q. Deficiency of Vitamin K can occur in which conditions?

A. Obstructive jaundice, antibiotic therapy, and administration of dicoumarol.
Q. What is the mechanism of action of dicoumarol?
A. It competitively inhibits Vitamin K epoxide reductase.

Q. So, dicoumarol is used for what purpose?

A. To prevent intravascular thrombosis.
Q. Excess dicoumarol will produce what?
A. Bleeding tendency.

Q. Which substance will inhibit Vitamin K?

A. Dicoumarol.

Q. Excess dose of Vitamin K in neonates may lead to which condition?

A. Hemolysis and jaundice.

Q. Bleeding tendency is common in the deficiency of which?

A. Vitamin K, Vitamin C, and platelets.

Vitamin-II: Water soluble vitamins

Q. What is the source of thiamine?
A. Aleurone layer of cereals (food grains) is a rich source of thiamine. Whole wheat
flour and unpolished rice and yeast are very good sources.

Q. Thiamine pyrophosphate is required for which reactions ?

A. Transketolase, pyruvate dehydrogenase, and alpha keto glutarate dehydrogenase.

Q. Which Vitamin is required for oxidative decarboxylation?

A. Thiamine pyrophosphate.

Q. In thiamine deficiency, what alterations are seen in blood ?

A. Increased pyruvic acid level and increased transketolase activity.

Q. What are the clinical manifestations of thiamine deficiency?

A. Beriberi, Wernick.s syndrome, and polyneuritis.

Q. Beberi is due to the deficiency of which Vitamin?

A. Thiamine.

Q. What is the daily requirement of Vitamin B1 (thiamine) ?

A. 1 to 1.5 milligram.

Q. Chronic alcoholism may lead to the deficiency of which Vitamin?

A. Vitamin B1.
Q. Wernicke.s encephalopathy is due to the deficiency of which Vitamin?
A. Vitamin B1.

Q. What is the co-enzyme function of riboflavin ?

A. FMN and FAD dependent enzymes.
Q. What are the FAD dependent enzymes?
A. Succinate dehydrogenase, acyl CoA dehydrogenase, xanthine oxidase,
glutathione reductase, glycine cleavage system, pyruvate dehydrogenase, and alpha
ketoglutarate dehydrogenase.

Q. What are the manifestations of riboflavin deficiency?

A. Glossitis, cheilosis, angular stomatits, and circumcorneal vascularisation.

Q. What is the dietary sources of riboflavin?

A. Rich sources are liver, dried yeast, egg, and milk.

Q. What is the daily requirement of riboflavin?

A. 1.5 mg per day.

Q. Which Vitamin is synthesised in the body?

A. Niacin.

Q. What is the co-enzyme function of niacin?

A. NAD and NADP.

Q. Name some important NAD dependent enzymes.

A. Lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, pyruvate
dehydrogenase, beta hydroxy acyl CoA dehydrogenase, and mitochondrial isocitrate
dehydrogenase.

Q. Name the NADPH generating reactions.

A. Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, malic
enzyme, and cytoplasmic isocitrate dehydrogenase.

Q. What are the important NADPH utilizing reactions?

A. Beta keto acyl ACP dehydrogenase, alpha, beta unsaturated ACP dehydrogenase,
HMGCoA reductase, met-hemoglobin reductase, dihydrofolate reductase, and
phenylalanine hydroxylase.

Q. Pellagra is seen in the deficiency of which Vitamin?

A. Niacin.

Q. What are the features of pellagra ?

A. Dermatitis, diarrhea, and dementia.
Q. What is the precursor of niacin?
A. Tryptophan.

Q. Tryptophan will give rise to how much niacin?

A. About 60 mg of tryptophan will yield 1 mg of niacin.

Q. Tryptophan is deficient in which food stuff?

A. Maize and corn.

Q. Which conditions will lead to symptoms of pellagra?

A. Isoniazid therapy, low tryptophan content in diet, niacin deficiency, hartnup disease,
and carcinoid syndrome.

Q. What is the dietary sources of niacin?

A. Natural sources of niacin are dried yeast, rice polishing, liver, peanut, whole cereals,
legumes, meat and fish. About half of the requirement is met by the conversion of
tryptophan to niacin. About 60 mg of tryptophan will yield 1 mg of niacin.

Q. What is the daily requirement of niacin?

A. The R.D.A is 20 mg/day.

Q. Transamination reaction requires which Vitamin?

A. Pyridoxal phosphate.

Q. Pyridoxal phosphate is required for what reactions?

A. Transamination reactions, decarboxylation of amino acids, ALA synthase, glycogen
phosphorylase.

Q. Give an example of transamination reaction.

A. Alanine transaminase (ALT) will catalyse the reaction, alanine to pyruvate.

Q. What is its clinical significance?

A. Blood level of ALT is increased in liver diseases, AST is increased in myocardial
infarction.

Q. Give some examples of decarboxylation reactions.

A. Glutamate to GABA (gamma aminobutyric acid), histidine to histamine, 5-hydroxy
tryptophan to serotonin, cysteine to taurine, and serine to ethanol amine.

Q. Xanthurenic acid in urine is seen in the deficiency of which Vitamin?

A. Pyridoxal deficiency.

Q. What are the manifestations of pyridoxal deficiency?

A. Infantile convulsions, peripheral neuritis, pellagra, and anemia.
Q. What is the reason for infantile convulsions in pyridoxal deficiency?
A. Pyridoxal phosphate is required for the formation of GABA, and it is an inhibitory
neurotransmitter, absence of which leads to hyper-excitation and convulsions.

Q. What is the reason for peripheral neuritis in pyridoxal deficiency?

A. PLP is involved in the synthesis of sphingolipids, so B6 deficiency leads to
demyelination of nerves and consequent peripheral neuritis.
Q. What is the reason for pellagra-like disease in pyridoxal deficiency?
A. Since niacin is produced from tryptophan, one of the enzymes of this pathway is PLP
dependent. So B6 deficiency in turn leads to niacin deficiency which is manifested as
pellagra.

Q. Can you give an exmple of one Vitamin deficiency leading to another Vitamin
deficiency?
A. PLP deficiency in turn leads to niacin deficiency which is manifested as pellagra.

Q. What is the reason for anemia in pyridoxal deficiency?

A. PLP is required for ALA synthase. In adults hypochromic microcytic anemia may
occur due to the inhibition of heme biosynthesis.

Q. What are the drugs which cause pyridoxal deficiency?

A. Isonicotinic acid hydrazide (INH) (isoniazid), cycloserine, penicillamine and oral
contraceptives act as B6 antagonists. Ethanol in the body is converted to acetaldehyde,
which inactivates PLP.

Q. What are the dietary sources of pyridoxal?

A. Rich sources are yeast, rice polishing, wheat germs, cereals, legumes (pulses),
egg, milk, meat, fish and green leafy vegetables.

Q. What is the daily requirement of pyridoxal phosphate?

A. 1 to 2 mg/day.

Q. What is the co-enzyme form of pantothenic acid?

A. Co-enzyme A.

Q. What is the function of CoA?

A. Oxidation of pyruvic acid and activation of acyl groups.

Q. Deficiency of pantothenic acid leads to what?

A. Burning foot syndrome.

Q. What are the donors for acetyl CoA pool?

A. Pyruvate, fatty acid, and amino acids.
Q. Acetyl CoA is used for what purposes?
A. Oxidation in TCA cycle, fatty acid synthesis, cholesterol synthesis, steroid
synthesis, and ketone body formation.

Q. Succinyl CoA is used for what purposes?

A. Oxidation in TCA cycle, heme synthesis, and activation of acetoacetate.

Q. What is the function of biotin?

A. Carboxylation reactions.
Q. Name some reactions dependent on biotin.
A. Acetyl CoA carboxylase, propionyl CoA carboxylase, and pyruvate carboxylase.

Q. What is the antagonist for biotin?

A. Avidin.

Q. What is its use in laboratory?

A. Biotin-avidin reaction is used in immunosorbent assays.

Q. What is the chemical nature of folic acid?

A. Pteroyl glutamic acid (pteridine + PABA + glutamic acid).

Q. What is PABA?
A. Para amino benzoic acid.

Q. What is the co-enzyme form of folic acid?

A. Tetrahydro folic acid.

Q. What is the main function of folic acid?

A. Tetrahydro folic acid is the carrier of one carbon units.

Q. What are the causes of folate deficiency?

A. Pregnancy, defective absorption (sprue, celiac disease), anticonvulsant drugs
(hydantoin, dilantin, phenytoin, phenobarbitone), hemolytic anemias, and dietary
deficiency.

Q. What is the major manifestation of folic acid deficiency?

A. Macrocytic anemia.

Q. Folic acid deficiency in pregnancy is associated with what?

A. Folic acid deficiency during pregnancy may lead to neural tube defects in the
fetus. Folic acid prevents birth defects (fetal malformations such as spina bifida).
Q. What are the other minor effects of folic acid?
A. Folic acid is also useful to reduce the level of homo-cysteine in blood, and
therefore helps in preventing heart diseases. Folic acid is beneficial in prevention of
cancer.

Q. What are the laboratory findings in folic acid deficiency?

A. (1) Normal folic acid level in serum is decreased. (2) FIGLU is excretion is more,
especially after histidine load. (3) AICAR excretion in urine. (4) Peripheral blood picture
shows macrocytic anemia. (5) Homocysteine level in blood is increased

Q. What are the sources of folic acid?

A. Yeast, liver, egg, green leafy vegetables, cereals, and pulses.
Q. What is the daily requirement of folic acid?
A. The RDA of free folate is 200 mg/day. In pregnancy the requirement is increased to
400 mg/day.

Q. What is the mechanism of action of sulphonamides?

A. They are anti-bacterial agents. They have structural similarity with PABA. Therefore
they competitively inhibit the enzyme responsible for the incorporation of PABA into folic
acid.

Q. What is the mechanism of action of trimethoprim?

A. It inhibits the folate reductase and so formation of THFA is reduced. It is bactericidal
agent.

Q. What is mechanism of action of methotrexate?

A. It inhibits folate reductase, and is a powerful anticancer drug.

Q. What are inhibitors of folic acid?

A. Methotrexate, trimethoprim, pyrimethamine and sulphonamide.

Q. Name a water soluble Vitamin, which is stored in the body.

A. Vitamin B12.

Q. What is the metal present in Vitamin B12?

A. Cobalt.

Q. What is the ring system present in Vitamin B 12?

A. Corrin ring.

Q. Vitamin B12 is absorbed from where?

A. Ileum.

Q. What is the transport form of Vitamin B12?

A. Methyl B 12.
Q. What is the carrier of Vitamin B12 in blood?
A. Transcobalamin-II, a glycoprotein, is the specific carrier.

Q. What is the storage form of Vitamin B12?

A. It is stored in the liver cells, as ado-B12 form, in combination with transcobalamin-I or
transcorrin.

Q. What is the co-enzyme function of Vitamin B 12?

A. Methyl malonyl CoA isomerase, and homocysteine methyl transferase.

Q. What abnormalities are seen in Vitamin B 12 deficiency?

A. Methyl malonic aciduria, accumulation of methyl malonic acid, breakdown of myelin
sheaths and interruption in nerve transmission. Homocysteinuria is also seen.

Q. What abnormal compound is excreted in Vitamin B12 deficiency?

A. Methyl malonic acid in urine.

Q. What is folate trap?

A. The production of methyl THFA is an irreversible step. Therefore, the only way for
generation of free THFA is methyl THFA to THFA, by a Vitamin B12 dependent step.
When B12 is deficient, this reaction cannot take place. This is called the methyl
folate trap.

Q. What is the clinical importance of folate trap?

A. This leads to the associated folic acid scarcity in B12 deficiency.

Q. What is the explanation of demyelination in Vitamin B12 deficiency?

A. In Vitamin B12 deficiency, there is non-availability of active methionine.
Therefore, methylation of phosphatidyl ethanolamine to phosphatidyl choline is not
adequate. This leads to deficient formation of myelin sheaths of nerves.

Q. What are the causes of B12 deficiency?

A. Nutritional B12 deficiency, decrease in absorption, addisonian pernicious
anemia, atrophy of gastric epithelium, and pregnancy.

Q. What is the cause for pernicious anemia?

A. It is an autoimmune disease with a strong familial background. Antibodies are
generated against intrinsic factor. So IF is deficient, leading to defective absorption
of B12.

Q. What are the manifestations of Vitamin B12 deficiency?

A. Megaloblastic anemia and subacute combined degeneration.
Q. What is the difference in folate deficiency and B12 deficiency?
A. In folate deficiency, there is macrocytic anemia, and in B12 deficiency, there is
additional neurological symptoms also.

Q. What is the daily requirement of Vitamin B12?

A. One to two microgram/per day.

Q. A patient who has undergone gastrectomy is likely to develop deficiency of which

Vitamin?
A. Vitamin B12.

Q. In Vitamin B12 deficiency, what are the abnormalities seen in urine?

A. Urine may contain methyl malonic acid, homocystine, cystathione, and formimino
glutamic acid.

Q. Which is the Vitamin totally absent in plant sources?

A. Vitamin B12.

Q. What are the sources of Vitamin B12?

A. Liver, meat, fish, and curd.

Q. What is the chemical structure of Vitamin C?

A. L-ascorbic acid.

Q. How it is synthesised?
A. Man and primates cannot synthesise ascorbic acids. Lower animals could
synthesise it from glucose through glucuronic acid pathway.

Q. What are the major functions of ascorbic acid?

A. Ascorbic acid promotes collagen formation through its action on post-
translational hydroxylation of proline and lysine residues.

Q. What are the other functions of ascorbic acid?

A. Parahydroxy phenyl pyruvate oxidation to homogentisic acid, iron absorption from the
intestine, reconversion of methemoglobin to hemoglobin, and adrenal steroidogenesis.

Q. Which Vitamin is required for post-translational modifications?

A. Ascorbic acid.

Q. What is the daily requirement of ascorbic acid?

A. 75 mg per day.

Q. Scurvy is due to the deficiency of which Vitamin?

A. Ascorbic acid.
Q. What are the important features of scurvy?
A. Hemorrhagic tendency, microcytic anemia, bone pain, bleeding gums.

Mineral Metabolism
Q. What influences absorption of calcium from intestine?
A. Vitamin D, calcitriol, parathyroid hormone, phytic acid, and oxalate.

Q. What is the daily requirement of calcium?

A. 500 mg per day.

Q. What are the sources of calcium?

A. Milk, egg, fish, and vegetables.

Q. What is the function of calcium ?

A. Coagulation, neuromuscular activity, intracellular messenger, activation of
enzymes, and bone formation.

Q. What is the normal level of calcium in blood?

A. 9-11 mg /dl.

Q. Which will influence serum calcium level?

A. Calcitriol, calcitonin, and parathyroid hormone.

Q. How parathyroid hormone regulates calcium level in blood?

A. Bone resorption, increased absorption of calcium from intestines, and increased
absorption of calcium from renal tubules.

Q. Hypocalcemia results in what clinical condition?

A. Tetany.

Q. What is the reason for tetany?

A. Hypoparathyroidism.

Q. What are the features of hyperparathyroidism ?

A. Osteoporosis, hypercalciuria, and urinary calculi.

Q. What is the normal level of phosphorus in blood.

A. 3-4 mg /dl.

Q. What is the normal level of sodium in blood ?

A. 136-145 mEq/L.
Q. What is the important extracellular cation?
A. Sodium.

Q. Which will control the sodium level in serum?

A. ADH, aldosterone, and cortisone.

Q. What is the normal level of potassium in blood ?

A. 3.5 to 5 mEq /L.

Q. What is the major intracellular cation?

A. Potassium.

Q. What is the manifestation of hypokalemia?

A. In ECG, T wave inverted, ST segment is lowered.

Q. What is the normal level of chloride in blood ?

A. 96- 106 mEq /L.

Q. What is the daily requirement of iron for a normal adult male ?

A. 10-20 milligram per day.

Q. What are the dietary sources of iron ?

A. Green leafy vegetables, meat, and jaggery.

Q. Which is the trace element, deficient in milk?

A. Iron.

Q. What are important iron containing proteins?

A. Hemoglobin, myoglobin, cytochromes, catalase, tryptophan pyrrolase, xanthine
oxidase, transferrin, and ferritin.

Q. Which will increase iron absorption from intestines?

A. Gastric HCl, ascrobic acid, and cysteine.

Q. What are the factors which will retard iron absorption?

A. Phytic acid (in cereals) oxalic acid (in leafy vegetables), calcium, zinc, lead and
phosphates.

Q. Iron is absorbed from which part?

A. Upper part of duodenum.
Q. How is iron absorbed?
A. Iron in the intestinal lumen enters the mucosal cell in the ferrous state. This is bound
to transferring molecule present in brush border surface of intestinal cell. One transferrin
molecule can bind with two atoms of iron. This is then complexed with a specific
receptor. This iron-transferrin receptor is internalised.

Q. How iron absorption is regulated?

A. Iron metabolism is unique because homeostasis is maintained by regulation at the
level of absorption and not by excretion. When iron stores in the body are depleted,
absorption is enhanced. When adequate quantity of iron is stored, absorption is
decreased. This is referred to as .mucosal block. of regulation of absorption of iron.

Q. What is the carrier protein in iron in blood?

A. Transferrin.

Q. Which enzyme will help in iron carriage in blood?

A. Ferroxidase (ceruloplasmin).

Q. What is the storage form of iron?

A. Ferritin.

Q. What is hemosiderin?
A. Excess iron is loaded as hemosiderin.

Q. What is haptoglobin?
A. It is the carrier of free hemoglobin.

Q. What is hemopexin?
A. It is the carrier of free heme.

Q. Anemia is resulted in the deficiency of which substances?

A. Iron, copper, vitamin C, folic acid, vitamin B12, and pyridoxal phosphate.

Q. Iron deficiency results in what?

A. Microcytic hypochromic anemia.

Q. What are the features of hemosiderosis?

A. Cirrhosis of liver, diabetes mellitus, and yellow colour of skin.

Q. What is the cause for hemosiderosis?

A. Repeated transfusion of whole blood.

Q. What are the important copper containing enzymes?

A. Ceruloplasmin, cytochrome oxidase, cytochrome C, tyrosinase, lysyl oxidae, and
super oxide dismutase.
Q. What are dietary sources of copper?
A. Cereals, meat, and liver.

Q. What is ceruloplasmin?
A. It is ferroxidase, and it promotes oxidation of ferrous ion to ferric form.

Q. What are the characteristic features of Wilson.s hepatolenticular degeneration?

A. Ceruloplasmin level in blood is decreased, copper excretion is reduced, and copper
is accumulated in liver to produce cirrhosis.

Q. What is the daily requirement of iodine?

A. 150-200 microgram.

Q. What is the daily requirement of zinc?

A. 15-20 milligram.

Q. What are the important enzymes which contain zinc?

A. Alkaline phosphatase, amylase, carbonic anhydrase, and RNA polymerase. Zinc is
required for insulin secretion.

Q. What is Fluorosis?
A. It is produced when fluoride concentration in water is more than 20 ppm.
Osteoporosis is the manifestation.

Q. What is the importance of selenium?

A. It is an anti-oxidant.

Q. Name the selenium containing enzyme.

A. Glutathione peroxidase.

Energy Metabolism and Nutrition

Q. What is the calorific value of carbohydrates?
A. Four kilocalories per gram.

Q. What is the calorific value of fats?

A. Nine kilocalories per gram.

Q. How much calories are generated per gram of fat ?

A. kCal.

Q. What is the respiratory quotient?

A. It is the ratio of carbon dioxide produced to the oxygen consumed.
Q. What is the respiratory quotient of carbohydrates?
A. One.

Q. What is the respiratory quotient for a mixed diet?

A. About 0.82.

Q. What is specific dynamic action?

A. Increased heat production after intake of food.

Q. Which foodstuff has maximum specific dynamic action ?

A. Proteins.

Q. Basal metabolic rate is increased in which conditions?

A. Fever, starvation, cold climate, and increased thyroid hormones.

Q. Increased basal metabolic rate is observed in which clinical condition?

A. Grave.s disease (hyperthyroidism).

Q. What are the beneficial effects of dietary fibre?

A. Increased motility of intestine, decreased absorption of cholesterol, and increased
glucose tolerance.

Q. Name an undigestible carbohydrate.

A. Pectin.

Q. Which food stuffs contain polyunsaturated fatty acids?

A. Vegetable oils, sunflower oil, and groundnut oil.

Q. Name essential fatty acids.

A. Linoleic acid, linolenic acid, and arachidonic acid.

Q. What is the dietary advice for a patient with hypercholesterolemia?

A. They should take polyunsaturated fatty acids.

Q. What foodstuffs contain cholesterol?

A. Egg, butter, ghee, and pig fat.

Q. A patient with coronary artery disease is advised to refrain from what?

A. Egg.

Q. What is the recommended daily allowance of protein of a normal adult?

A. 1 g/kg.

Q. Negative nitrogen balance is observed in which conditions?

A. Chronic infection, old age, and malnutrition.
Q. Positive nitrogen balance is observed in which conditions?
A. Pregnancy, convalescence, and growth period.

Q. Lysine is deficient in which foodstuff?

A. Pulses.

Q. Phenyl alanine is deficient in which food stuff?

A. Tapioca.

Q. Methionine is deficient in which food stuff?

A. Cereals.

Q. How all amino acids are made available in a mixed diet?

A. Supplementation by combining cereals and pulses.

Q. What are the salient features of Kwashiorkor?

A. Hypoalbuminemia, hypomagnesemia, growth retardation, lethargy, and loss of
appetite.

Q. How much energy is required for a 60 kg person, with sedentary work?

A. 2000 kCal.

Q. A balanced diet should have calories for carbohydrate, proteins and fats in which
ratio?
A. 60:20:20.

Detoxification and Biotransformation of

Xenobiotics
Q. What is detoxification process?
A. Biochemical processes whereby noxious substances are rendered less harmful
or more water soluble and easily excretable.

Q. What are xenobiotics?

A. They are compounds accidentally ingested or taken as drugs or compounds
produced in the body by bacterial metabolism.

Q. Give an example of a substance detoxified by reduction.

A. Para nitro phenol.

Q. Give examples of substances detoxified by hydrolysis.

A. Acetanilide to aniline + acetate, aspirin to salicylic acid + acetate.
Q. Give names of conjugating agents.
A. PAPS, UDP glucuronic acid, glutathione, and glycine.

Q. Give some examples of substances detoxified by conjugation.

A. Bilirubin to bilirubin glucuronide, phenol to phenyl sulfate, and benzoic acid to
hippuric acid.

Q. Which amino acids are used for detoxification?

A. Glutamine, glycine, and cysteine.
Q. Give examples of substances detoxified by sulfation.
A. Phenol to phenyl sulfate, and indole to indoxyl sulfate.

Q. What is the sulfating agent?

A. PAPS (phospho adenosyl phospho sulfate).

Q. How benzoic acid is detoxified?

A. Benzoic acid + glycine = benzoyl glycine or hippuric acid.

Q. How epinephrine is excreted?

A. As methyl conjugates.

Q. What is the methylating agent?

A. S-adenosyl methionine.

Q. What is the most common environmental poison?

A. Lead.

Q. What are common causes of lead poisoning?

A. Paint, lead containig petrol, lead pipes, news papers, xerox copies and
cigarette smoke are important contaminants.

Q. What are the occupations in which persons are prone to get lead poisoning?
A. Battery repair, radiator repair, soldering, painting and printing.

Q. What is the toxic level of lead?

A. Blood level of lead, more than 10 ?g/dl in children and more than 25 ?g/dl in
adults lead to toxic manifestations.

Biochemical Aspects of Environmental

Pollution
Q. What are the manifestations of chronic lead poisoning?
A. Miscarriage, stillbirth, and premature birth. In children, mental retardation, learning
disabilities, behavioral problems, hyperexcitability and seizures are seen. Anemia,
abdominal colic and loss of appetite are very common.

Q. What are the manifestation of acute lead poisoning?

A. Encephalopathy, convulsions, mania, neuropathy, abdominal colic, severe anemia
and kidney damage, discolouration and blue line along the gums.

Q. When does acute toxicity is manifested?

A. If the blood level of lead is more than 70 mg/dl, acute toxicity is manifested.
Q. What is the cause of anemia in lead poisoning?
A. Lead inhibits delta amino levulinic acid (ALA) synthase, ALA-dehydratase and
ferrochelatase. So, heme synthesis is blocked. Life span of RBC is shortened. Anemia
enhances lead absorption, lead in turn produces more anemia, thus a vicious cycle is
operating.

Q. What are the antidotes for lead poisoning?

A. Calcium dodecyl edetate (Calcium disodium versenate), penicillamine and
dimercaprol (BAL) are used as antidotes. Dimercaptosuccinic acid is a better but costly
antidote.

Q. What is the pH of 0.1 M hydrochloric acid?

A. One.

Q. When pH falls by 1 unit, what is the change in the hydrogen ion concentration?
A. Increases by 10 times.

Q. Relationship between pH and pK is given by which equation?

A. Henderson-Hasselbalch.s equation.

Q. What determines the pH of buffer?

A. By the ratio of salt to acid.

Q. Buffer is most effective when?

A. When pK of the acid is nearer to pH.

Q. When is the buffering capacity is more?

A. When the absolute concentrations of salt and acid are more.

Acid Base Balance and pH

Q. In the blood, which buffer is most effective?
A. Bicarbonate buffer.

Q. What are the mechanisms for maintaining the normal pH of plasma?

A. Buffers of plasma, lung mechanism, and kidney mechanism.

Q. What is the alkali reserve of the body?

A. Bicarbonate is the alkali reserve.

Q. What is the ratio of bicarbonate to carbonic acid in blood?

A. Bicarbonate to carbonic acid ratio is 20.

Q. What are the mechanisms by which renal regulation of acid load is achieved?
A. Excretion of hydrogen ions in urine, excretion of ammonium ions in urine, and
production of bicarbonate in renal tubules.

Q. Glutaminase enzyme is used for what purpose?

A. For production of ammonia in kidney tubules.

Q. What is metabolic acidosis?

A. Primary deficit of bicarbonate.

Q. What are the causes of metabolic acidosis?

A. Diabetic ketosis, chronic renal failure, and diarrhea.

Q. What are the features of diabetic ketoacidosis?

A. Lowered bicarbonate, elevated plasma chloride, and increased anion gap.

Q. What is the formula used to calculate anion gap?

A. (sodium + potassium) minus (chloride + bicarbonate).

Q. What is the cause for high anion gap acidosis?

A. Diabetic ketoacidosis, chronic renal failure, renal tubular acidosis, lactic acidosis.

Q. What is metabolic alkalosis?

A. Primary excess of bicarbonate.

Q. What are the causes of metabolic alkalosis?

A. Prolonged vomiting, gastric aspiration, and ingestion of antacids.

Q. What is respiratory acidosis?

A. Primary excess of carbonic acid.

Q. What are the causes of respiratory acidosis?

A. Bronchial asthma, bronchopneumonia, and narcotic poisoning.
Q. What is respiratory alkalosis?
A. Primary deficit of carbonic acid.

Q. What is the cause for respiratory alkalosis?

A. Hyperventillation.

Q. What are the results of prolonged vomiting?

A. Alkalosis, hypochloremia, and hypokalemia.

Electrolyte and Water Balance

Q. What is the major intracellular cation?
A. Potassium.

Q. What is the major extracellular cation?

A. Sodium.

Q. What is the function of anti diuretic hormone?

A. Its secretion is stimulated when plasma osmolarity increases, ADH decreases
the urine output, and retains water in the body.

Q. What are the factors regulating fluid and electrolyte balance?

A. Aldosterone and anti diuretic hormone.

Q. What are the diuretic drugs used?

A. Aldosterone antagonists, angiotensin converting enzyme inhibitors, and carbonic
anhydrase inhibitors.

Q. What is the major cause for isotonic contraction of ECF?

A. Small intestinal obstruction.

Q. What are the causes for hypotonic contraction of ECF?

A. Infusion of dextrose (without saline), Addison.s disease.

Q. What are the causes for hypertonic contraction of ECF?

A. Diarrhoea, vomiting.

Q. What are the causes for isotonic expansion of extracellular fluid?

A. Congestive cardiac failure and hyperaldosteronism.

Q. What is the cause for hypotonic expansion of extracellular fluid?

A. Inappropriate secretion of ADH.
Q. What is the important cause for hypertonic expansion of ECF?
A. Cushing.s syndrome.

Q. What are the metabolic imbalances seen in diarrhea?

A. Metabolic acidosis, hypertonic contraction of ECF, urine with high specific gravity,
and urine output reduced.

Q. What is a nucleotide?
A. Nitrogenous base + sugar + phosphate.

Q. What is a nucleoside?
A. Nitrogenous base + sugar.

Q. What are the sugars?

A. Ribose in RNA and deoxyribose in DNA.

Q. What are the bases present in nucleotides?

A. Purines and pyrimidines.

Q. Name the common purines.

A. Adenine and guanine.

Q. Name the common pyrimidines.

A. Cytosine, uracil, and thymine.

Molecular Biology-I: Nucleotides, Chemistry

and Metabolism
Q. What are the bases present in DNA?
A. Adenine, guanine, cytosine, and thymine.

Q. Which nitrogenous base is absent in DNA?

A. Uracil.

Q. Which base is found exclusively in DNA and not in RNA?

A. Thymine.

Q. Which base is found exclusively in RNA and not in DNA?

A. Uracil.

Q. Which amino acid is required for both purine and pyrimidine synthesis?
A. Aspartic acid and glutamine.
Q. N3 of purine ring is donated by what?
A. Glutamine.

Q. Glycine donates what part of the purine ring?

A. C4, C5, N7 atoms.

Q. N1 atom of purine ring is coming from what?

A. Aspartic acid.

Q. One carbon pool donates which carbon atoms of purine ring?

A. C2 and C8 carbon atoms.

Q. What is the key enzyme of de novo synthesis pathway of purines?

A. The committed step in de novo synthesis is the reaction catalysed by
amidotransferase (step 1).

Q. How is de novo synthesis of purine regulated?

A. Amidotransferase enzyme is inhibited by AMP and GMP.

Q. What are the enzymes needed for salvage pathway of purines?

A. Adenine phospho ribosyl transferase (APRTase) and hypoxanthine guanine
phospho ribosyl transferase (HGPRTase).

Q. What is the importance of the salvage pathway?

A. This is of special importance in tissues like RBCs and brain where the de novo
pathway is not operating.

Q. What is the clinical significance of the purine analogues?

A. They act as cell cycle inhibitors and can be used as anti-cancer drugs.

Q. Give a few examples of purine analogues, used as anti-cancer drugs.

A. 6-mercapto-purine inhibits the conversion of IMP to GMP and AMP. 2. Cytosine
arabinoside. 3. Folate antagonists (Methotrexate) would affect the reactions involving
one carbon group transfers. 4. Azaserine is a glutamine antagonist and
therefore inhibits reactions involving glutamine.

Q. What is the end product of catabolism of purines in human beings?

A. Uric acid.

Q. What is xanthine oxidase?

A. It is the enzyme for the reactions, hypoxanthine to xanthine and xanthine to uric acid.
Q. What is the speciality in this reaction?
A. Xanthine oxidase is a metalloflavoprotein containing FAD, molybdenum and iron.
As xanthine is oxidised to uric acid, hydrogen peroxide (reactive oxygen species) is
produced.

Q. What is the normal uric acid level in blood?

A. The normal blood level of uric acid ranges from 2-5 mg/dl in females and 3-7 mg/dl in
males.

Q. What is the normal excretion rate of uric acid?

A. The daily excretion of uric acid varies from 500-700 mg.

Q. Which property of uric acid is responsible for the manifestations of gout?

A. Uric acid is sparing soluble in water.

Q. Increased uric acid level is seen in which conditions?

A. Gout, pre-eclampsia, Hodgkin.s lymphoma, leukemia, and diabetic ketoacidosis.

Q. Hyperuricemia can result from defect of which enzymes?

A. Ribosyl amido transferase, PRPP synthetase, HGPRTase, APRTase, Glucose-6-
phosphatase, and glutathione reductase.

Q. Hyperuricemia is observed in which conditions?

A. Gout, Lesch Nyhan syndrome, von Gierke.s disease.

Q. What are salient features of Lesch-Nyhan syndrome?

A. Self mutilation, hyperuricemia, and X-linked inheritance.

Q. What is the mechanism of action of allopurinol?

A. It is an analogue of hypoxanthine. It inhibits xanthine oxidase, and thereby
decreasing the formation of uric acid.

Q. It is what type of inhibition?

A. Xanthine oxidase converts allopurinol to alloxanthine. It is a more effective
inhibitor of xanthine oxidase. This is a good example of .suicide inhibition.

Q. Hypouricemia can result from deficiency of which enzyme?

A. Adenosine deaminase deficiency.

Q. How is it manifested?
A. Severe immunodeficiency.

Q. What are used for pyrimidine synthesis?

A. Carbamoyl phosphate and aspartic acid.
Q. What is the rate limiting step in pyrimidine synthesis?
A. Aspartyl trans carbamoylase.

Q. What is carbamoyl phosphate synthetase II and how is it different from type I

enzyme?
A. CPS-II is involved in pyrimidine synthesis, but CPS-I is for urea synthesis. CPS-II
is in cytosol, but CPS-I is in mitochondria. CPS-II is inhibited by CTP, whereas CPS-I is
not.

Q. How is pyrimidine synthesis pathway regulated in mammals?

A. CPS II is inhibited by CTP.

Q. What is the mechanism of action of 6-mercpto purine?

A. It inhibits conversion of IMP to AMP, and so acts as an antimetabolite.

Q. What is the mechanism of action of 5-fluorouracil?

A. It inhibits conversion of dUMP to dTTP, and acts as an antimetabolite.

Q. Orotic aciduria is a feature of deficiency of which enzymes?

A. OMP decarboxylase, OPRTase, and ornithine transcarbamoylase.

Q. What are the characteristic features of orotic aciduria ?

A. Megaloblastic anemia, urinary tract obstruction, and response to oral uridine therapy.

Q. Formation of dTMP (thymine nucleotide) requires what enzyme and co-enzymes?

A. Methylation of dump is done by thymidylate synthase. The methyl group is
donated by methylene-THFA. Later, THFA is regenerated by dihydrofolate reductase,
using NADPH. Methotrexate inhibits dihydrofolate reductase and thereby reduces the
regeneration of THFA, and it is a powerful anticancer agent.

Q. How deoxyribonucleotides are formed?

A. By the reduction at the 2' carbon of the corres ponding nuceloside
diphosphates (NDP to dNDP).

Q. What are the enzymes and co-enzymes for this reaction?

A. Ribonucleotide reductase, NADPH, and thioredoxin.

Q. What are the important characteristics of Watson-Crick model of DNA?

A. Right-handed double helix, each turn of helix has 10 base pairs, Hydrogen bonds
between purines and pyrimidines, and DNA strands running in opposite directions
(anti parallel).

Q. What is base pairing rule?

A. Pairing (hydrogen bonding) of adenine with thymine and guanine with cytosine.
Purine is paired with pyrimidine A+T = G+C.
Q. What are the modifications seen in histones?
A. Acetylation, methylation, and phosphorylation.

Q. What is nucleosome?
A. DNA wrapped around histones.

Molecular Biology-II: DNA structure and

Replication

Q. What is euchromatin?
A. Transcriptionally active chromatin is called euchromatin. It is less densely
packed, and sensitive to digestion by DNAse.

Q. What is meant by DNA replication?

A. During cell division, each daughter cell gets an exact copy of the genetic information
of the mother cell. This process of copying the DNA is known as DNA replication.

Q. How the exact copying is effected?

A. Each strand serves as a template or mould, over which a new complementary
strand is synthesised. The base pairing rule is always maintained.

Q. What are the enzymes required for DNA replication?

A. DNA polymerase, topo isomerase, and DNA ligase.

Q. How many DNA polymerases are there in mammalian cells?

A. Five. Alpha, beta, gamma, delta, and epsilon.

Q. What a replisome?
A. DNA replication needs the participation of more than 20 enzymes and proteins,
collectively called DNA replicase system or replisomes.

Q. What is a replication bubble?

A. Helicases move on both directions, separating the strands in advance of the
replication. This forms a replication bubble.

Q. Replication is in which direction?

A. Polymerisation of the new strand of DNA is taking place from 5' to 3' direction.
This means that the template is read in the 3' to 5' direction.

Q. How replication starts?

A. An RNA primer, about 100-200 nucleotides long, is synthesised by the RNA primase.
Q. What is meant by semiconservative nature of replication?
A. In the daughter cell, one strand is derived from the mother cell, while the other strand
is newly synthesised. This is called semi-conservative type of DNA replication.

Q. What is meant by semi-discontinuous nature of replication?

A. DNA synthesis is always in the 5' to 3' direction in both strands. Replication fork
advances towards one side. So, in one strand, the replication is taking place
continuously, but in the other strand replication is in small pieces.

Q. What is lagging strand?

A. The strand which is discontinuously synthesized is referred to as the .lagging strand.
and the one continuously polymerised as the .leading strand..

Q. What are okazaki fragments?

A. The small DNA molecules attached to its own primer RNA in the lagging
strand are called okazaki fragments. The RNA is removed and DNA pieces are
joined by ligases.

Q. Xeroderma pigmentosum is due to deficiency of what process?

A. Defect in DNA repair mechanism (nucleotide excision repair).

Q. Defect in DNA repair mechanisms produce what clinical conditions?

A. Xeroderma pigmentosum, ataxia-telangectasia, Fanconi.s anemia, and Bloom.s
syndrome.

Q. Which enzymes protects cellular ageing?

A. Telomerase.

Q. In prokaryotes, DNA replication is inhibited by what drugs?

A. Ciprofloxacine, nalidix acid, and novobiocin.

Q. DNA replication in eukaryotes is inhibited by what drugs?

A. 5-fluoro uracil, 6-mercaptopurine, cytosine arabinoside, and etoposide.

Q. What is transcription?
A. The process of making a complementary mRNA copy of DNA.

Q. The mRNA is a complementary copy of which strand of DNA?

A. Template strand.

Q. What is coding strand?

A. The opposite strand of template strand. Coding strand has the same sequence as of
the mRNA.

Q. What is the enzyme necessary for the transcription?

A. DNA dependent RNA polymerase or RNAP.
Q. What are the different types of RNAP?
A. RNAP type II or B is the enzyme synthesizing mRNAs. RNAP type I or A is
responsible for synthesis of rRNA while type III or C is responsible for production
of tRNA.

Molecular Biology-III: Transcription and

Translation
Q. What is the specific inhibitor of RNAP?
A. RNAP II is inhibited by alpha amanitin.

Q. What is the direction of transcription?

A. It takes place in the 5' to 3' direction.

Q. What is TATA Box?

A. It is a signal for initiation of transcription in prokaryotes. It is about 10 bp
upstream of starting of mRNA synthesis. It is also called pribnow box.

Q. What is the corresponding signal in mammals?

A. Godberg-Hogness Box. It is located at -25 to -30 position.

Q. How termination of transcription is effected?

A. The specific signals are recognised by a termination protein, the Rho factor,
then the RNAP enzyme dissociates from DNA. There is also Rho Independent
Termination. This is effected by an interrupted invert repeat in DNA. This is transcribed.
So the mRNA makes a hairpin structure. This
obstructs further movement of RNA.

Q. What are post-transcriptional modifications?

A. Removal of introns, addition of a cap at 5' end, adding poly A tail at 3' end and
methylation.

Q. What are the non-coding sequences?

A. Leader sequence, poly-A tail, introns.

Q. What is intron?
A. Part of mRNA that is removed is called intron.

Q. What is a spliceosome?
A. Small nuclear ribonucleoprotein particles (SnRNPs) associated with hnRNA at
the exon ntron junction form spliceosomes. This is taking place inside the nucleus.
Q. What is the cause for systemic lupus erythematosis?
A. Production of auto antibodies against small nuclear ribonucleoprotein particles
cause systemic lupus erythematosis (SLE), a fatal autoimmune disease.

Q. What are ribozymes?

A. Enzymes made up of RNA are called ribozymes.

Q. Give some examples of ribozymes.

A. Spliceosomes, RNAse-P (which generates the ends of tRNAs) and peptidyl
transferase (present in ribosomes) are examples of ribozymes.

Q. Give the names of inhibitors of RNA synthesis.

A. Rifampicin, actinomycin, mitomycin and amanitin.

Q. What is the mechanism of action of mitomycin?

A. Actinomycin D and mitomycin intercalate with DNA strands, thus blocking
transcription. They are used as anticancer drugs.

Q. What is the mechanism of action of Rifampicin?

A. It binds to beta subunit of RNA polymerase, and inactivates it. Rifampicin is widely
used in the treatment of tuberculosis and leprosy.

Q. What is the mechanism of action of amanitin?

A. It inactivates RNA polymerase II.

Q. What is reverse transcriptase?

A. In retroviruses, RNA is the genetic material (not DNA). The RNA dependent, DNA
polymerase or reverse transcriptase will make a new DNA strand based on the RNA
template. Thus, genetic information is transferred from RNA to DNA.

Q. Give an example of retrovirus.

A. The human immunodeficiency virus (HIV) causing AIDS is a retrovirus.

Q. What are the structural features of tRNA molecule?

A. It has clover shape appearance. It contains unusual bases. Amino acid binding is at
3' end. The opposite part has anticodon arm.

Q. During protein synthesis, amino acid sequence is specified by what?

A. The codons present in messenger RNA.

Q. During replication, DNA is synthesised in which direction?

A. From 5' to 3' direction.

Q. During transcription, mRNA is synthesised in which direction?

A. From 5' to 3' direction.
Q. During translation, protein is synthesised in which direction?
A. From amino terminal end to carboxy terminal end.

Q. What are the salient features of genetic code?

A. Triplet codons are consecutive three bases pairs in mRNA. The codons are non-
overlapping, degenerate, but unambiguous and universal.

Q. What is meant by degeneracy of genetic code?

A. One amino acid is represented by multiple codons.

Q. What is meant by the term wobbling?

A. Anticodons pair with codons that differ at the third base.

Q. What is the initiating codon for protein synthesis?

A. AUG.

Q. What is Shine-Dalgarno sequence?

A. Marker of start signal for translation in bacterial mRNA.

Q. Where is protein biosynthesis taking place?

A. Ribosomal assembly either attached to endoplasmic reticulum, or in cytoplasm.

Q. How many high energy bonds are required for the synthesis of one peptide bond?
A. Four high energy bonds.

Q. Give examples of diseases caused by protein targetting defects.

A. Zellweger syndrome, adrenoleukodystrophy and primary hyperoxaluria.

Q. What is the function of signal peptide?

A. Causes anchorage of ribosome to endoplasmic reticulum, and so directs the new
protein into the endoplasmic reticulum. Such proteins are destined for secretion.

Q. What is the location of signal peptide?

A. In the amino terminal region of the nascent protein.

Q. What is the location of the address for destination of proteins?

A. These are in the carboxy terminal end of proteins.

Q. Give examples for post-translational modifications.

A. Gamma carboxylation of prothrombin, hydroxylation of proline in collagen,
methylation of histones, and glycosylation of proteins.

Q. Give examples of diseases produced by defect in post-translational modifications.

A. Lathyrism, Ehlers-Danlos syndrome, and scurvy.
Q. Give examples of inhibitors of translation in eukaryotic cells?
A. Puromycin, cycloheximide, diphtheria toxin, and ricin.

Q. What is the mechanism of action of erythromycin?

A. Inhibition of translocation in prokaryotes.

Q. What is the mechanism of action of tetracycline?

A. Inhibition of tRNA binding to ribosome in bacteria.

Q. What is the mechanism of action of streptomycin?

A. Misreading of codes and inhibition of initiation complex formation in bacteria.

Q. What is the mechanism of action of chloramphenicol?

A. Inhibition of peptidyl transferase in bacteria.

Q. Give examples of reversible inhibitors of protein synthesis in bacteria.

A. These antibiotics are bacteriostatic. Tetracyclins, chloramphenicol, erythromycin and
clindamycin are examples.

Q. Give an example of irreversible inhibitor of protein synthesis in bacteria.

A. These antibiotics are bactericidal. Streptomycin is an example.

Q. Leber.s hereditary optic neuropathy is due to what?

A. Due to mutation in mitochondrial DNA.

Q. Give examples of X-chromosome linked transmission.

A. Hemophilia, glucose-6-phsophate dehydrogenase deficiency, and duchenne type
muscular dystrophy.

Q. What is a mutation?
A. An alteration in the genetic material results in a mutation.

Q. Give an example.
A. HbS or sickle-cell hemoglobin is produced by a mutation of the beta chain in which
the 6th position is changed to valine, instead of the normal glutamate.

Q. What type of mutation is it?

A. Here, the normal codon GAG is changed to GUG (transversion).
Molecular Biology-IV: Molecular Genetics and
Control of Gene Expression
Q. Give an example for an unacceptable mutation.
A. Haemoglobin M.

Q. Give examples for mutagens.

A. Acridine orange, X-rays, gamma rays, and methyl cholanthrene.

Q. How mutagenecity of a compound is tested?

A. By Ame.s test.

Q. In which phase of the cell cycle, DNA synthesis is maximum?

A. S phase.

Q. What is the p53?

A. It is an oncosuppressor gene product.

Q. Give examples of enzyme induction.

A. Beta galactosidase by lactose, tryptophan pyrrolase by glucocorticoid and ALA
synthase by barbiturates.

Q. Give an example of repression.

A. ALA synthase by heme.

Q. Give names of some important antiviral drugs.

A. Acyclovir, Ribavirin, Zidovudine.

Q. What is a prion?
A. .Prions. is the acronym for .proteinaceous infective particles..

Q. What are the uses of recombinant DNA technology?

A. Quantitative preparation of bio-molecules, especially human proteins. Risk of
contamination is eliminated, when preparing such biomolecules. Specific probes for
diagnosis of diseases can be prepared. It is used in gene therapy.

Q. What are restriction endonucleases?

A. Restriction endonucleases are referred to as .molecular scissors.. These
enzymes recognize specific sequence with palindrome arrangement in the double
stranded DNA, and then cleave at those sites. They are useful in recombinant DNA
technology.
Q. What are required for preparing a recombinant DNA molecule?
A. Restriction endonuclease, plasmid vector, and DNA ligase.

Molecular Biology-V: Recombinant DNA

Technology and Gene Therapy
Q. How are DNA fragments separated?
A. Agarose gel electrophoresis.

Q. What is Southern blotting?

A. DNA is isolated, fragmented by restriction endonucleases, cut pieces are
electrophoresed in agarose gel, then blotted over to a nitrocellulose membrane, when
single-stranded DNA will be adsorbed in the nitrocellulose membrane. The radio
active probe is placed over the membrane. The membrane is then thoroughly washed
and autoradiographed.

Q. What is the use of Southern blotting?

A. To identify abnormal genes, to demonstrate virus integration, prenatal diagnosis.

Q. Give some examples of genetic diseases that could be identified by Southern

blotting.
A. Sickle cell anemia, Huntington.s chorea, Duchenne muscular dystrophy.

Q. What is Northern blotting?

A. The Northern blot is used to demonstrate specific RNA.

Q. What is Western blotting?

A. In this technique, proteins (not nucleic acids) are identified. The proteins are
isolated from the tissue and electrophoresis is done. The separated proteins are then
transferred on to a nitrocellulose membrane. After fixation, it is probed with
radioactive antibody and auto-radiographed.

Q. What is meant by the term cloning?

A. The term cloning has two broad meanings. When a gene of higher organism is
introduced into a bacterial DNA, it is called .cloning of the gene. or .molecular
cloning.. When a cell from an animal is grown to an exact duplicate of that
animal, it is known as .cloning of an animal. Or .somatic cloning..

Q. What are the applications of cloning of animals?

A. Animals with genetically desirable traits could be bred more efficiently, e.g. cows
yielding more milk. Cows or goats may be genetically engineered to produce milk
containing any human protein.
Q. RFLP (restriction fragment length polymorphism) is used for what?
A. Locating mutations in DNA.

Q. What is the application of DNA fingerprinting?

A. It has medico-legal application.

Q. What are the vectors used for gene therapy?

A. Retrovirus, adenovirus, and plasmid liposome complex.

Q. Give some diseases in which gene therapy is used successfully?

A. Severe combined immuno deficiency, duchenne muscular dystrophy, cystic
fibrosis, familial hypercholesterolemia, and hemophilia.

Q. What is transgenesis?
A. It is a form of germ cell gene therapy. A recombinant DNA segment,
containing the desired gene from another species, is introduced into the fertilized ova.
The embryos are allowed to develop in the uterus of another animal.

Q. What is the technique used for gene amplification?

A. Polymerase chain reaction.

Q. Which enzyme is required for PCR (polymerase chain reaction)?

A. Taq polymerase.

Q. What is reverse PCR?

A. This allows cDNA synthesis from mRNA followed by PCR amplification. In
ordinary PCR, DNA is detected, that DNA could be from a living or non-living
organism. But in reverse PCR, mRNA is detected, that means, it is derived from a
living organism.

Q. What is the use of PCR?

A. Diagnosis of bacterial and viral diseases, medicolegal cases, diagnosis of genetic
disorders, especially prenatal diagnosis. Only very minute quantity of sample is
required.

Q. What is the full form of AIDS?

A. Acquired immuno deficiency syndrome.

Q. What is the causative organism of AIDS?

A. Human immunodeficiency virus.

Q. How can you detect window period of the disease?

A. In the window period viral capsid antigen (p24) can be detected
Q. What are the usual laboratory findings in the diagnosis of AIDS?
A. The antibodies against gp120 are detected by the ELISA test. To rule out the false
positive test, the ELISA positive blood, is then retested with Western blot analysis.

Biochemistry of AIDS
Q. What other special tests could be done?
A. T-helper cell count is below 300/ cu.mm. By RTPCR (reverse transcriptase
polymerase chain reaction, the number of HIV particles in blood can be estimated, a
value of less than 5000 copies per ml of blood has good prognosis, while a count
more than 1 lakh per ml means very bad prognosis.

Q. HIV belongs to which group of virus?

A. It is a retrovirus. It is an RNA virus.

Q. What is the characteristic of retrovirus?

A. It contains the enzyme reverse transcriptase.

Q. How the virus gets entry into the tissue cells?

A. The gp 120 of the virus envelope will specifically bind with CD4 molecules on the
surface of target cells. CD4 acts as a receptor for the virus.

Q. Where is CD4 molecules present?

A. The CD4 molecules are present on the surface of T-helper cells.

Q. What are the major groups of anti-HIV drugs available?

A. Reverse Transcriptase (RT) inhibitors and protease inhibitors.

Q. How RT inhibitors are classified?

A. nucleoside analogues, non-nucleoside analogues and nucleotide analogues.

Q. Name some chemical carcinogens.

A. Methyl cholanthrene, aflatoxins, benzopyrenes.

Q. Name some physical carcinogens.

A. X-ray, gamma-ray and UV-ray.

Q. Name some anti-mutagens and anti-carcinogens.

A. Vitamin A, Vitamin C, Vitamin E, and curcumin.

Q. Name some oncogenic viruses.

A. Epstein Barr virus (EBV), hepatitis B virus(HBV), and human papilloma virus.
Q. What are Oncogenes?
A. Genes capable of causing cancer. Oncogenes are specific sequences in DNA which
when expressed may produce cancer.

Q. What are proto-oncogenes?

A. Oncogenes present in normal cells are also called as proto-oncogenes.

Biochemistry of Cancer
Q. Proto-Oncogenes may be activated by what mechanisms?
A. Viral infection, mutation in proto-oncogene, promoter insertion, and chromosome
translocation.

Q. Name a cancer, produced by the deletion of an oncosuppressor gene?

A. Retinoblastoma.

Q. What are tumour markers?

A. They are factors released from the tumour cells, which could be detected in blood
and therefore indicate the presence of the tumour in the body.

Q. What is the clinical application of tumour markers?

A. They are useful for the following purposes. (1) For follow up of cancer and to
monitor the effectiveness of the therapy. (2) To detect the recurrence of the tumour

Q. Name some important tumour markers.

A. Alpha feto protein, carcino embryonic antigen, prostate specific antigen, neuron
specific enolase, beta chain of human chorionic gonadotropin, and regan iso-enzyme of
alkaline phosphatase.

Q. Alpha feto protein (AFP) level in serum is increased in which condition?

A. Hepatoma.

Q. Carcino embryonic antigen level is increased in which type of cancers?

A. Colorectal and gastrointestinal cancers.

Q. What is the significance of beta chain of human chorionic gonadotropin?

A. It is a tumour marker for choriocarcinoma.

Q. What is the mechanism of action of mitomycin?

A. Intercalation with DNA strands.

Q. What is the mechanism of action of Methotrexate?

A. It is a folic acid antagonist.
Q. What is vincristine and vinblastine?
A. They are alkaloids from vinca rosea, they interfere with assembly of cytoskeleton and
inhibits stathmokinesis (spindle movement), so they are used as anti-cancer drug.

Q. What is the mechanism of action of adriamycin?

A. It inhibits topo-isomerase.

Q. What is an Isotope?
A. Isotopes of a given element will have different atomic weights, but will have
same atomic number.

Q. Radiation hazard is mainly due to which type of radiation?

A. Alpha radiation.

Q. Iodine-125 emits mainly emits which type of radiation?

A. Gamma radiation.

Q. What is the isotope used for DNA studies?

A. P-32.

Q. P-32 is used clinically for what purpose?

A. To treat polycythemia vera.

Applications of Radio-isotopes in Medicine

Q. Which radio-active compound is used to measure glomerular filtration rate (GFR)?
A. 131-Iodine labelled hippuran.

Q. For RIA (radio immuno assay), the radio-active isotope used is:
A. 125-Iodine.

Q. What is the use of radio active radium in medicine?

A. Intracavity application of radiation, such as carcinoma cervix or body of uterus.

Q. What is the common source of radiation in teletherapy?

A. 137-Cs (caesium) with a half-life of 30 years.

Q. What are radiosensitive tumours?

A. Lymphomas, Hodgkin.s disease and neuroblastoma are highly radiosensitive.

Q. What are the important toxic effects of radiation?

A. Leukopenia, thrombocytopenia, and radiation dermatitis.
Q. How lactose is synthesised?
A. UDP glucose is epimerased to UDP galactose. Then the galactose unit is
transferred from UDP galactose to glucose. This synthesis of lactose in
mammary gland is catalysed by lactose synthase.

Q. How lactose synthesis is regulated?

A. The lactose synthase has two subunits, a catalytic subunit which is a galactosyl
transferase and a modifier subunit that is alpha lactalbumin. The level of the modifier
subunit is under the control of prolactin.

Q. What is the major difference between human and cow.s milk?

A. Human milk has higher carbohydrate content than cow.s milk while protein content is
less.

Q. How is to humanize cow.s milk?

A. To humanise cow.s milk, protein is to be diluted and carbohydrate is to be added.
Thus, to one cup of cow.s milk, add half a cup of water and two teaspoons of sugar.
This will make it comparable to human milk.

Body Fluids
Q. Milk contains which type of fatty acids?
A. The fatty acids are mainly saturated, but 50% of them are medium chain fatty acids
(Lauric and Myristic acids).

Q. What is the advantage of medium chain fatty acids?

A. They are easily digested, absorbed and metabolized.

Q. What is the major protein in cow.s milk?

A. Eighty percent protein of cow.s milk is casein.

Q. What type of protein is casein?

A. It is a phospho-protein.

Q. How the phosphate group is attached to protein?

A. The phosphate groups are added to the hydroxyl groups of serine or threonine
residues.

Q. What is whey?
A. If milk is acidified and pH lowered to 4.7, the casein is precipitated (iso-electric
precipitation). The supernatant is called whey.
Q. What are the proteins present in whey?
A. Lactalbumin, lactoglobulin and lysozyme.

Q. What are G proteins?

A. They are involved in signal transduction.

Q. How the G proteins work?

A. The receptors are in membrane, and binding of hormone causes activation of G
protein.

Q. How is G protein activated?

A. Binding of hormone on receptor causes attachment of GTP to G protein, and
thereby G protein is activated.

Q. What is the function of activated G protein?

A. Activated G protein activates adenyl cyclase.

Q. What is the function of adenyl cyclase?

A. Adenyl cyclase will produce cyclic AMP.

Q. How adenyl cyclase is destroyed?

A. By phospho diesterase.

Hormones-I: Mechanism of Action of Hormones

Q. How cyclic AMP further works?
A. Cyclic AMP activates protein kinase.

Q. What is the function of protein kinase?

A. It phosphorylates enzymes or target proteins, so that they are activated.

Q. Name some hormones which act through cyclic AMP as the second messenger.
A. Glucagon, ACTH, TSH, ADH, FSH, LH.

Q. Name some second messengers.

A. Cyclic AMP, 1,2-diacyl glycerol, inositol triphosphate, and calcium.

Q. Name some hormones which act through cyclic GMP as the second messenger.
A. ANF (atrial natriuretic factor).

Q. Name some hormones that bind to intracellular receptors.

A. Glucocorticoids, mineralocorticoids, estrogens, progesterone, androgens, and
thyroxin.
Q. What are hypothalamic neuropeptides?
A. These neurohormones are antidiuretic hormone (ADH) and oxytocin.

Q. Name the important hypothalamic releasing factors.

A. TRH (thyrotropin releasing hormone), GnRH (gonadotropin releasing hormone),
GHRH (growth hormone releasing hormone), somatostatin (growth hormone inhibitory
factor), CRF (corticotropin releasing factor), and PIF (prolactin inhibitor factor).

Q. Alpha chain of human chorionic gonadotropin (HCG) is shared with what else?
A. TSH, FSH, LH and HCG have the common alpha chain, and beta chains are specific.

Hormones-II: Pituitary Hormones

Q. What are the hormones produced by anterior pituitary?
A. GH (Growth hormone), ACTH (Adrenocorticotropic hormone), LH (Luteinising
hormone), FSH (Follicle stimulating hormone), TSH (Thyroid stimulating hormone),
MSH (Melanocyte stimulating hormone), and PRL (Prolactin).

Q. What is the major effect of growth hormone?

A. GH increases the uptake of amino acids by cells, enhances protein synthesis, and
produces positive nitrogen balance. The anti-insulin effect of GH causes lipolysis
and hyperglycemia. The overall effect of GH is to stimulate growth of soft tissues,
cartilage and bone. It is anabolic.

Q. Increased secretion of growth hormone will lead to what condition?

A. Excess secretion of GH secretion leads to gigantism in children and acromegaly
in adults.

Q. What is the result of decreased growth hormone secretion?

A. Deficiency of GH secretion in early childhood results in pituitary dwarfism.

Q. What is the function of FSH?

A. FSH stimulates growth of ovarian follicles in females and spermatogenesis (Sertoli
cells) in males.

Q. What is the function of LH?

A. Testosterone in males (secreted by Leydig interstitial cells) and progesterone in
females (secreted by corpus luteum), are increased under the influence of LH.

Q. The 11-hydroxylase is required for the synthesis of which hormone?

A. Cortisol.

Q. The 17-hydroxylase is required for the synthesis of which hormones?

A. Cortisol, testosterone, and estradiol.
Q. Which is the precursor of steroid hormones?
A. Cholesterol.

Q. What are the hormones produced from progesterone?

A. Corticosterone, aldosterone, testosterone, and estrogens.

Q. Cortisol has how many carbon atoms?

A. 21.

Q. Aldosterone has how many carbon atoms?

A. 21.

Hormones-III: Steroid Hormones

Q. Testerone has how many carbon atoms?
A. 19.

Q. Estrogen has how many carbon atoms?

A. 18.

Q. What is the immediate precursor of estrogens?

A. Testosterone.

Q. What are the structural features of estradiol?

A. Cyclopentanophenanthrene ring, total 18 carbon atoms, aromatic character of A ring,
and hydroxyl groups on 3rd and 17 carbon atoms.

Q. 21-hydroxylase is required for the synthesis of which hormone?

A. Aldosterone.

Q. What are the effects of glucocorticoids?

A. Increased gluconeogenesis, augmented lipolysis, elevated protein breakdown, and
depressed immune function

Q. What is the precursor of thyroxin?

A. Tyrosine.

Q. Name some antithyroid agents.

A. Thiocyanate, perchlorate, and methimazole.

Q. How thyroid hormones are produced?

A. Tyrosine residues of thyroglobulin are iodinated.
Q. What is the function of thyroid stimulating hormone?
A. It increases the uptake of iodine by thyroid gland, enhances the oxidation of iodine to
iodide, and favours the hydrolysis of thyroglobulin to produce T4.

Q. What is the ratio of T4 and T3 in blood?

A. Blood concentration of T4 is 70 times more than of T3.

Hormones-IV: Thyroid Hormones

Q. What are the functions of thyroid hormones?
A. Calorigenic effect or thermogenesis and BMR is increased.

Q. How this is produced?

A. The thermogenic effect is mediated by uncoupling of oxidative phosphorylation.
Thyroxine in large quantities can swell the mitochondria. Basal metabolic rate (BMR)
is increased.

Q. What are the biochemical features of thyroid hormones?

A. Thyroxine increases cellular metabolism. Gluconeogenesis and carbohydrate
oxidation are increased. Glucose tolerance test shows rapid absorption. Fatty acid
metabolism is increased.

Q. Deficiency of thyroxine results in which condition?

A. Myxedema.

Q. What are the salient features of hypothyroidism?

A. Decreased T3 level, increased TSH level, lethargy, hypercholesterolemia, weight
gain, and decreased basal metabolic rate.

Q. What are the characteristic features of primary hyperthyroidism?

A. High TSH and T4 levels, increased rate of metabolism, weight loss, tachycardia,
fine tremors, sweating, diarrhea, emotional disturbances, anxiety and sensitivity to heat.

Q. Why sodium fluoride is used as a preservative of blood for glucose estimation?

A. To prevent glycolysis and to prevent loss of sugar.

Q. What are the preservatives used in urine sample?

A. Formalin, thymol, chloroform, toluene, concentrated HCl and glacial acetic acid are
the commonly used urine preservatives.

Q. What is optical density?

A. Optical density = minus logT.
Q. What is Beer-Lambert.s law?
A. As per Beer.s law, the intensity of the colour is directly proportional to the
concentration of the coloured particles in the solution. The Lambert.s law states that the
amount of light absorbed by a coloured solution depends on the length of the column or
the depth of the liquid through which light passes.

Clinical Biochemistry-I
Q. What is end point analysis?
A. Serum sample and reagents are mixed and incubated for a fixed time, to develop
the colour optimally. Then, the OD is ascertained and the concentration of the
substances is calculated. This is called end point analysis.

Q. What is kinetic method?

A. Serum and reagents are incubated, and readings are taken at 2 and 3 minutes
exactly, and from the difference in OD between the two values, the concentration is
calculated. Here the optimum colour is not developed, but is quicker and hence is
often used in autoanalysers.

Q. What is accuracy?
A. Accuracy is the closeness of a result to the true value.

Q. What is meant by the term precision?

A. Precision refers to the reproducibility of the result. Precision depends on the
technique, the reagents, as well as on the technician.

Q. What is meant by specificity?

A. Specificity of a reaction denotes that only one substance will answer that
particular test. Specificity is determined by the method of the analysis.

Q. What is the normal serum bilirubin level?

A. 0.2 to 0.8 mg/dl.

Q. What is the normal blood level of unconjugated bilirubin?

A. 0.2-0.6 mg/dl.

Q. What is the normal serum level of conjugated bilirubin?

A. Less than 0.2 mg/dl.

Q. What is latent jaundice?

A. Serum bilirubin between 1 mg/dl and 2 mg/dl.

Q. Jaundice appears at what level of bilirubin?

A. Jaundice appears if the serum bilirubin goes above 2 mg/dl.
Clinical Biochemistry-II: Liver and Gastric
Function Tests
Q. What is meant by van den Bergh.s direct positive test?
A. When bilirubin is conjugated, the purple colour is produced immediately on mixing
with the reagent, the response is said to be van den Bergh.s direct positive.

Q. What is indirect positive van den Bergh.s test?

A. When the bilirubin is unconjugated, the colour is obtained only when alcohol is
added, and this response is known as indirect positive.

Q. What type of bilirubin is present in hemolytic jaundice?

A. In hemolytic jaundice, unconjugated bilirubin is increased in serum. Hence van den
Bergh.s test is indirect positive.

Q. What happens in obstructive jaundice?

A. In obstructive jaundice, conjugated bilirubin in serum is elevated, and van den
Bergh.s test is direct positive.

Q. What about hepatocellular jaundice?

A. In hepatocellular jaundice, a biphasic reaction is observed, because both conjugated
and unconjugated bilirubins are increased in serum.

Q. What are important liver function tests?

A. Serum bilirubin, albumin, alkaline phosphatase, urine bile salts, bile pigments and
urobilinogen.

Q. Increase in serum unconjugated bilirubin occurs in which condition?

A. Hemolytic jaundice.

Q. What are the features of obstructive jaundice?

A. Elevated conjugated bilirubin in plasma, presence of bile salts and bile pigments in
urine, increased alkaline phosphatase level in blood, and increased cholesterol in blood.

Q. Which tests will be positive in a urine of a patient with obstructive jaundice?

A. Gmelin.s test, Hay.s test, and Fouchet.s test.

Q. What are the enzymes useful in diagnosis of liver diseases?

A. Alanine amino transferase, alkaline phosphatase, and gamma glutamyl transferase.

Q. What are the salient laboratory findings in a patient with chronic liver disease?
A. Serum albumin is lowered, albumin globulin ratio is reversed, and prothrombin time is
prolonged.
Q. What is the characteristic laboratory findings in alcoholic cirrhosis?
A. Elevation of gamma glutamyl transferase level in serum.

Q. What are the important stimulants for gastric acid secretion?

A. Gastrin, vagus stimulation, and histamine.

Q. What is alkaline tide?

A. When HCl is produced in stomach, bicarbonate level within the cell increases
(formed from H2CO3), it is reabsorbed into blood stream. This would account for the
alkaline tide of plasma and urine, immediately after meals.

Q. What is the maximal gastric acid output?

A. It is the acid output in millimol per hour, after the stimulation.

Q. What is the upper limit of maximal gastric acid output?

A. 30 mmol/ hour in females and 45 mmol/hour in males.

Q. What is basal acid output?

A. It is the acid output in millimol per hour, in the absence of all intentional stimulation.

Q. What is the upper limit of basic acid output?

A. 5 millimol/hour in females and 10 millimol in males.

Q. Hypo-acidity is found in which conditions?

A. Pernicious anemia, carcinoma of stomach, and atrophic gastritis.

Q. How much is glomerular filtration rate?

A. 120-125 ml per minute.

Q. What is the function of glomerulus?

A. An ultrafiltrate of the blood is produced in glomerulus, while the cells and
proteins are retained in the blood.

Q. What is the normal renal threshold value for glucose?

A. Blood level of 180 mg/ dl.

Q. What is the normal specific gravity of urine?

A. 1.015 to 1.025.

Q. What is the minimum and maximum specific gravity of urine?

A. 1.003 to 1.032.
Clinical Biochemistry-III: Kidney Function Tests
Q. What is the specific gravity of urine in chronic renal failure?
A. Fixed to 1.010.

Q. Specific gravity of urine increased in which condition?

A. Acute glomerulonephritis.

Q. Polyuria is seen in which conditions?

A. Diabetes mellitus, diabetes insipidus, and chronic renal failure.

Q. What are the features of chronic renal failure?

A. Urine with fixed specific gravity of 1.010, polyuria, increased blood urea and
creatinine.

Q. Name abnormal substances seen in urine.

A. Protein, blood, sugar, ketone bodies, bile salts, bile pigments, and urobilinogen.

Q. Proteinuria is seen in which conditions?

A. Acute glomerulo nephritis, nephrotic syndrome, pyelonephritis, and multiple myeloma

Q. Which test is commonly employed to detect urinary protein?

A. Heat and acetic acid test.

Q. What is micro-albuminuria?
A. When small quantities of albumin (50-300 mg/ day) is seen in urine.

Q. How proteinurias are classified?

A. Glomerular proteinuria, overflow proteinuria, nephron loss proteinuria, tubular
proteinuria, and urogenic proteinuria.

Q. What is meant by renal clearance?

A. Clearance is defined as the quantity of blood or plasma completely cleared of a
substance per unit time and is expressed as milliliter per minute. It is the ml of plasma
which contains the amount of that substance excreted by the kidney within a
minute.

Q. How renal plasma flow is measured?

A. Para amino hippurate (Diodrast) clearance.

Q. What is the correct method for assessing glomerular filtration rate?

A. Inulin clearance.
Q. What is its disadvantage?
A. Inulin has to be infused intravenously throughout the test period.

Q. What is the normal value for PAH clearance ?

A. About 700 ml/min.

Q. What is the best method for assessing glomerular filtration rate?

A. Creatinine clearance test.

Q. What is the advantage of creatinine test?

A. Creatinine is formed spontaneously (non-enzymatic), so the blood level and
excretion rate of creatinine is a constant from day to day.

Q. What is the normal value of creatinine clearance?

A. In males 85-125 ml/min and in females 80-115 ml/min.

Q. What is the significance of creatinine clearance?

A. A decreased creatinine clearance is a very sensitive indicator of a reduced
glomerular filtration rate.

Q. What is the normal creatinine level in blood?

A. For adult males, 0.7-1.4 mg/dl, for adult females, 0.6-1.3 mg/dl.

Q. What is creatinine coefficient?

A. It is the urinary creatinine expressed in mg/kg body weight.

Q. What is the significance of creatinine coefficient?

A. The value is elevated in muscular dystrophy.

Q. What is the normal value of creatinine coefficient?

A. Normal range is 20-28 mg/kg for males and 15-21 mg/kg for females.

Q. Urea clearance is lowered in which condition?

A. Chronic liver failure.

Q. What is the maximum urea clearance value?

A. 75 ml/minute.

Q. What is the standard urea clearance value?

A. 54 ml/minute.

Q. When do you call it standard urea clearance?

A. When the volume of urine formed is less than 2 ml per minute.

Q. What is the normal blood urea level?

A. 20-40 mg /dl.
Q. What is the clinical significance of increased urea level in blood ?
A. Urea level is increased in renal failure.

Q. How failure of concentrating capacity of urine is measured ?

A. Concentration test (Water deprivation test).

Q. How is tubular concentrating capacity measured?

A. Urine specific gravity.

Q. What are the usual tests to assess tubular function?

A. Measurement of specific gravity, concentration test, dilution test, acidification test.