MLAB 2401: Clinical Chemistry

Keri Brophy-Martinez

Overview:
Amino Acids & Proteins
Amino Acids
● Building blocks of proteins
● Chemical properties determine
biological activity
● Origin
◦ Majority made in the human
⚫Generated from amino acid pool
⚫Generated from breakdown of proteins
◦ Essential Amino acids
⚫Ingested in diet
Amino Acids
● Linkedtogether by peptide bonds to
form the building blocks of proteins

Peptide
bond
Aminoacidopathies
• Rare inherited disorders
• Enzyme defect that inhibits the body’s
ability to metabolize certain amino acids
• Abnormality due to problem with enzyme
activity or the membrane transport
system for amino acids
• Cause severe medical problems due to
the buildup of toxic amino acids and/or
byproducts of amino acid metabolism in
blood
Aminoacidopathies: Disorders
– Phenylketonuria
• Absence of phenylalanine hydrolase
• Mousy odor of the urine
• Causes significant brain damage
– Tyrosinemia
• Three types
• Type I most severe
• Causes liver and kidney damage, affects CNS
– Alkaptonuria
• Absence of homogentisate oxidase
• Urine turns brownish-black upon exposure to
air
Aminoacidopathies: Disorders
– Maple syrup urine disease
• Absence or reduction of alpha-ketoacid
decarboxylase
• Hallmark feature is the odor of maple syrup or
burnt sugar in the urine, breath and skin
– Isovaleric Acidemia
• Absence of isovaleryl-CoA dehydrogenase
• Distinctive odor of sweaty feet due to build up of
isovaleric acid
Aminoacidopathies: Disorders

– Homocystinuria
• Absence of cystathionine-beta-synthetase

– Cystinuria
• Defect in amino acid transport system
• Results in the formation of stones
Proteins
• Built from one or more chains of amino
acids

• Specific

• Contain carbon, hydrogen, oxygen, sulfur

and nitrogen

• Nucleotide sequence in the genes dictates

the amino acid sequence of the protein
Proteins
● Synthesis
◦ Plasma proteins made in liver then
secreted by hepatocyte into circulation
◦ Immunoglobulins made in plasma cells
◦ Insufficient dietary quantities of amino
acids will limit synthesis and lower body
levels of proteins
Proteins
● Catabolism (Breakdown)
◦ Goal is to remove nitrogen from the
system
◦ Occurs in the digestive tract, kidneys, and
liver
◦ Produces ammonia, then urea
⚫Urea excreted via urine
◦ Produces ketoacids
⚫Ketoacids converted to glucose or fat
Structure of Proteins
Denaturation
● Disruption of structure
● Results in loss of function and protein
chemical properties
● Caused by:
◦ Heat
◦ pH changes
◦ Mechanical forces
◦ Exposure to UV light
◦ Exposure to chemicals
Classification of Proteins
● Simple proteins
◦ Proteins made of only amino acids
◦ Further classified as globular or fibrous
● Conjugated proteins
◦ Proteins with nonprotein groups attached
◦ Metalloproteins
◦ Lipoproteins
◦ Glycoproteins
◦ Mucoproteins
◦ Nucleoproteins
◦ Phosphoproteins
 Functions of Proteins
Protein Function Examples
Enzymes Catalyse chemical reactions Transminases,
phosphatases,
dehydrogenases
Hormones Chemical messengers that Insulin, growth hormone,
control the actions of cortisol
specific cells or organs
Transport Proteins Transport ions, small Hemoglobin, albumin,
molecules or transferrin
macromolecules across
biological membranes
Immunoglobulins Mediate humoral immune IgG, IgM, IgA
response to id and
neutralize foreign objects
Structural Structures of cells and Collagen, elastin, keratin
tissues
 Functions of Proteins
Protein Function Examples

Storage Serve as reserves of metal ferritin

ions and amino acids

Energy Reserve source of energy

Osmotic Force Maintain water distribution albumin

between cells and tissue,
interstitial compartments
and the vasculature
References
● Bishop, M., Fody, E., & Schoeff, l. (2010). Clinical
Chemistry: Techniques, principles, Correlations.
Baltimore: Wolters Kluwer Lippincott Williams &
Wilkins.
● http://www.stanford.edu/group/pandegroup/folding/
education/prstruc.html
● Sunheimer, R., & Graves, L. (2010). Clinical
Laboratory Chemistry. Upper Saddle River:
Pearson .