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CASE 2 LACTOSE INTOLERANCE

TIM AKADEMIK DIVISI SOOCA

2012

CASE REVIEW

Baby boy, 3.5months

CC : watery diarrhea

CASE REVIEW Baby boy, 3.5months CC : watery diarrhea History taking Physical Examination Lab Examination •
CASE REVIEW Baby boy, 3.5months CC : watery diarrhea History taking Physical Examination Lab Examination •
CASE REVIEW Baby boy, 3.5months CC : watery diarrhea History taking Physical Examination Lab Examination •
CASE REVIEW Baby boy, 3.5months CC : watery diarrhea History taking Physical Examination Lab Examination •

History taking

Physical Examination

Lab Examination

exclusive breast feed stopped 2

weeks ago and re- placed with formula milk

milk’s bottle has been sterilized

milk brand several times

2 days ago and baby has lesser diarrhea freq., looks better

iritable

looks thirsty

eyelid sunken

turgor

anal rash (+)

routine faeces

in normal limit

no bacteria

and abnormality on faeces

in normal limit • no bacteria and abnormality on faeces baeen changing given breastfeed Diagnosis :
in normal limit • no bacteria and abnormality on faeces baeen changing given breastfeed Diagnosis :
in normal limit • no bacteria and abnormality on faeces baeen changing given breastfeed Diagnosis :
in normal limit • no bacteria and abnormality on faeces baeen changing given breastfeed Diagnosis :
in normal limit • no bacteria and abnormality on faeces baeen changing given breastfeed Diagnosis :
in normal limit • no bacteria and abnormality on faeces baeen changing given breastfeed Diagnosis :

baeen changing

given breastfeed

Diagnosis : Lactose Intolerance

changing given breastfeed Diagnosis : Lactose Intolerance Treatment: pharmacology : - nonpharmacology : give the baby

Treatment:

pharmacology : - nonpharmacology : give the baby breast- feed

definition & classification

affecting factors

characteristics

mechanism

structure

function

kinetics

sunken eyes

turgor

enzyme

loose water & fluid

loose water & fluid

content & comparison of formula & breast milk

MECHANISM

looks thirsty

water by osmosis releasesattracts

baby boy, 3.5 months

lactose intolerance

lactase deficiency

watery diarrhea

abdominal pain

in large intestine

irritable

ETIOLOGY congenital cause

Treatment, BHP, PHOP, CRP

lactic acid

fermentation of lactose by colonic bacteria

formula milk

+

mutation in the LCT gene

bloating

H2

breast milk contains lactose + lactase enzyme lactose is digested & absorbed easily in small
breast milk
contains lactose + lactase enzyme
lactose is digested & absorbed
easily
in small intestine
absorbed by epithelial cell
normal digestive system
absorbed by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break
absorbed by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break
absorbed by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break
absorbed by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break
absorbed by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break
absorbed by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break
anal rash
anal rash
anal rash
anal rash

anal rash

anal rash
by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break down
by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break down
by epithelial cell normal digestive system anal rash contains lactose without lactase unable to break down
contains lactose without lactase unable to break down lactose in small intestine
contains lactose without lactase
unable to break down
lactose
in small intestine
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
when the baby drinks
when the baby drinks
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when
system anal rash contains lactose without lactase unable to break down lactose in small intestine when

1. Explain the definition and classification on enzyme

2. Describe the basic structure of enzyme

3. Explain the characteristics and kinetics of enzyme

4. Explain the mechanism of of action

5. Explain enzyme activator and inhibitor

6. Explain factors affecting enzyme activity

7. Explain the function of enzyme

8. Describe the clinical implication of enzyme assess- ment

9. BHP: patient’s rights, including to receive info about lab assessment implications

10. PHOP: education on detecting the disease

BASIC SCIENCE

ENZYME

DEFINITION A protein molecule that catalyses chemical reaction of other substances without itself being destroyed or altered upon completion of the reactions; functions in acceleration of chemical reactions

CLASSIFICATION

1. Oxidoreductases: oxidation-reduction reaction

2. Transferases: transfer of an atom, or group of, between 2 molecules (donoracceptor)

3. Hydrolases: hydrolytic cleavage of C-C, C-N, C-O by adding water molecule

4. Lyase: cleavage of C-C, C-N, and C-O bond by means other than hydrolysis or oxidation

5. Isomerase: catalyze geometrical/structural changes, rearrange bond structure of a com- pound to its isomers

6. Ligases: joining of 2 molecules coupled with the breakdown of phyrophosphate in ATP

BASIC STruCTurE

Holoenzyme An enzyme that has apoenzyme & coenzyme. Some enzymes are purely protein, but some of them do not need coenzyme

are purely protein, but some of them do not need coenzyme tight, stable protein apoenzyme :
are purely protein, but some of them do not need coenzyme tight, stable protein apoenzyme :
are purely protein, but some of them do not need coenzyme tight, stable protein apoenzyme :
are purely protein, but some of them do not need coenzyme tight, stable protein apoenzyme :
are purely protein, but some of them do not need coenzyme tight, stable protein apoenzyme :
are purely protein, but some of them do not need coenzyme tight, stable protein apoenzyme :

tight, stable

protein apoenzyme: inactive protein compo- nent of holoenzyme separable from the prosthetic group (coenzyme)

nonprotein

binds transciently

cofactor

bond

separable from the prosthetic group (coenzyme) nonprotein binds transciently cofactor bond prosthetic group coenzyme
separable from the prosthetic group (coenzyme) nonprotein binds transciently cofactor bond prosthetic group coenzyme
separable from the prosthetic group (coenzyme) nonprotein binds transciently cofactor bond prosthetic group coenzyme

prosthetic

group

coenzyme

Prosthetic group

ƒ Very stable, binds with covalent or noncovalent bonds

ƒ E.g.: Pyidoxal phosphate, Navin mononucleotide, FAD, metal ion Co, Cu, Mg, Mn, Zn most common prosthetic group

ƒ Enzyme-metal ion bond: metalloenzyme

ƒ Function:

Š Facilitate substrate binding and orientation

Š Covalent bond formation

Š Act as Lewis acid/base to render substrate electrophilic (e -) or neucleo- philic (e +) = more reactive

Cofactor

ƒ Same function as prosthetic group

ƒ Transcient, dissociable bond

ƒ Must be present in enzyme’s medium

ƒ Commonly metal ion (metal-activated enzymes)

Coenzyme

ƒ Definition: an organic nonprotein molecule, frequently phosphorylated deriva- tive of water-soluble vitamin

ƒ Function:

Š Transport substrates from point of generation to point of utilization

Š stabilizes substrate in aqueous env. of cell

CHArACTErISTICS

Have active sites: special 3-dimension pocket/cleft complimentary to substrate

Very efficient: turnover number Kcat

Highly specific: interacting with one or few substrates & catalyzes 1 type of chemi- cal reaction

Can be regulated (activated/inhibited) according to cell’s need

are localized in specific organelles within the cell

KINETICS

Consists of:

ƒ ES complex formation

ƒ Modification of substrate into product (still bound to enzyne)

ƒ release of product

Equation

complex formation ƒ Modification of substrate into product (still bound to enzyne) ƒ release of product

Michaelis-Menten Equation Describes how reaction velocity varies with substrate concentration

how reaction velocity varies with substrate concentration With Km = Michaelis-constant (k-1+k2/k1) Special notes: ƒ

With Km = Michaelis-constant (k-1+k2/k1) Special notes:

ƒ Km shows affinity of enzyme and substrate

ƒ Velocity is proportional to [E]

ƒ If [S] < Km : Vo ≈ [S]

ƒ Jika [S] > Km : Vo constant, ≈ Vmax

Lineweaver-Burk plot

> Km : Vo constant, ≈ Vmax • Lineweaver-Burk plot MECHANISM 1. Catalysis by proximity •

MECHANISM

1.

Catalysis by proximity

The shorter the distance greater rate of reaction

Orients substrate in position to react

2.

Catalysis by strain Enzyme breaking the covalent bond in substrate puts substrate in position that will put strain on bond bond will be vulnerable to cleavage

3.

Acid-Base Catalysis

r-side chains/prosthetic group can help catalysis by acting as acid or base (proton do- nor/acceptor)

SPECIFIC ACID-BASE CATALYST: only involves H+ atau OH- ions in surroundings

GENErAL ACID-BASE CATALYST: involves proton acceptor & donor from other mol-

ecules

4.

Covalent Catalysis Ketika suatu gugus pada Substrat berikatan kovalen dengan enzim, sehingga gugus ini dapat ditransfer ke substrat lain untuk membentuk produk baru -> “ping-pong mech- anism”

ACTIVATOr & INHIBITOr Activator: any substrate that can change an enzyme’s active site to increase the enzyme’s affinity towards substrate.

Inhibitor: any substance that can diminish the velocity of an enzyme-catalyzed reaction.

INHIBITOr

INHIBITOr IrrEVErSIBLE rEVErSIBLE • Covalent bond • noncovalent bond • Chemically alters enzyme • Inhibitor can
INHIBITOr IrrEVErSIBLE rEVErSIBLE • Covalent bond • noncovalent bond • Chemically alters enzyme • Inhibitor can
INHIBITOr IrrEVErSIBLE rEVErSIBLE • Covalent bond • noncovalent bond • Chemically alters enzyme • Inhibitor can

IrrEVErSIBLE

rEVErSIBLE

Covalent bond

noncovalent bond

• Chemically alters enzyme • Inhibitor can contaminate enzyme, even after inhibitor is moved to
• Chemically alters enzyme
• Inhibitor can contaminate enzyme, even after
inhibitor is moved to medium
COMPETITIVE
• Substrate-analog, binds to active site
• This inhibition can be overcome by adding
[S] until substrate can bind to active site
• E.g.: malonat as inhibitor of succinate
competes for the active site of succinate
dehydrogenase
competitive
inhibitor
uNCOMPETITIVE
• Binds to enzyme only when
substrate is already bound
to enzyme
• Binds to site other than
active and allosteric

NON-COMPETITIVE

Not substrate-analog, binds to allos- teric site

Changes active-site - thus substrate can not bind to it

[S] addition doesn’t affect velocity

E.g.: Cyanide binds to prosthetic group Cu2+ of cytochrome oxidase enzyme

non-competitive inhibitor
non-competitive
inhibitor

AFFECTING FACTOrS

1. pH: An enzyme’s optimal pH depends on the enzyme itself. Extremes of pH can also lead to denaturation of the enzyme

2. Substrate concentration: rate of reaction increases with substrate consentration until vmax is reached (enzyme is saturated)

3. Enzyme concentration: rate of reaction increases with enzyme consentration, and vice versa. Only a small amount of enzyme is needed to catalyze large amount of substrates

4. Temperature: reaction velocity increases with temperature until peak velocity is reached, further elevation decreases velocity (as result of enzyme denaturation)

5. Cofactor: required nonprotein component oof enzyme. Inorganic coenzyme, organic Fe2+, Zn2+, Ca2+

6. Konsentrasi Ion H+: H+ concentration shows equilibrium of enzyme denaturation on extremes of pH and the effect on enzyme, substrate, or both

FuNCTION Catalyses chemical reaction proceeding 10^3 to 10^8 times faster than uncatalyzed reac- tions. Typically each enzyme is capable of transforming 100-1000 substrate into product per second

CLINICAL IMPLICATION The possibility that enzymes can be used as markers for disease is based on:

Some enzymes are found only in specific/limited number of tissues with unequal

amount of activities (e.g. glutamate dehydrogenasi is more active in liver than heart)

Many enzymes can be detected in plasma/serum. Increase of tissue specific enzyme

in blood indicates tissue damage

Functional Plasma Enzyme: enzymes secreted into plasma that function there. Injury

to the producing organs cause decrease/cessation of activity (e.g. cholinesterase)

Non-functional Plasma Enzyme: intracellular enzymes that function there. Only

found in plasma in significant quantities when cells are damaged as consequent of leaky cell membranes If concentration of particular enzyme in a tissue is normally high, damage to a tissue will cause release into plasma of a high concentration of this enzyme. Minimal damage cytoplasmic enzymes leak out. Extensive damage + mitochondrial enzymes will be released.

BrEASTFEEDING

1. Lactation

Definition: production & secretion of breast milk to nourish the infant.

Hormones: Prolactin (milk production), oxytocin (ejection of milk into the duct)

2. Nutrition during infancy

Infants grow fast during the first year; their energy requirement is twice that of an adult, based on body weight. After 6 months, the infants’ energy needs decline.

3. Breast Milk

Breast milk is more easily and completely digested than formula milk

The carbohydrate in breast milk and formula is typically the same

The amount of protein in breast milk is less than that in cow’s milk. Calcium con- tent of breast milk is ideal for infants’ bone growth.

4. Benefits of Breastfeeding:

For Infants

ƒ Provides the appropriate composition and balance of nutrients

ƒ Lowering probability in Sudden Infant Death Syndrome (SIDS)

ƒ Improves cognitive development

ƒ Protects against variety of infections, food allergies

• For Mothers

ƒ Helps woman to lose weight after pregnancy.

ƒ May protect against breast and ovarian cancer

BHP: PATIENT’S RIGHTS

KODEKI (KODE ETIK KEDOKTErAN INDONESIA)

Pasal 7 :Seorang dokter hanya memberi surat keterangan dan pendapat yang telah

diperiksa sendiri kebenarannya.

Pasal 7c; Seorang dokter harus menghormati hak-hak pasien, hak-hak sejawatnya, dan hak tenaga kesehatan lainnya, dan harus menjaga kepercayaan pasien.

PATIENT’S rIGHTS

1. uu no. 44 Tahun 2009 : uu tentang rumah Sakit pasal 31 dan 32

meminta konsultasi tentang penyakit yang dideritanya kepada dokter lain yang

mempunyai Surat Izin Praktik (SIP) baik di dalam maupun di luar rumah Sakit;

mendapat informasi yang meliputi diagnosis dan tata cara tindakan medis, tujuan

tindakan medis, alternatif tindakan, risiko dan komplikasi yang mungkin terjadi, dan prognosis terhadap tindakan yang dilakukan serta perkiraan biaya pengobatan

2. uu no. 29 Tahun 2004 : uu tentang Praktik Kedokteran pasal 50 dan 51: Mendapatkan penjelasan secara lengkap tentang tindakan medis sebagaimana dimaksud dalam pasal 45 ayat (3), yaitu :

Diagnosis dan tata cara tindakan medis;

Tujuan tindakan medis yang dilakukan;

Alternatif tindakan lain dan resikonya;

risiko dan komplikasi yang mukin terjadi; dan

Prognosis terhadap tindakan yang dilakukan.

WMA INTErNATIONAL CODE OF MEDICAL ETHICS: DuTIES OF PHYSICIANS TO PATIENTS A physician shall owe his/her patients complete loyalty and all the scientific resources available to him/her. Whenever an examination or treatment is beyond the physician’s capacity, he/she should consult with or refer to another physician who has the necessary ability.

PHOP: EDUCATION ON DETECT- ING THE DISEASE

Providing/guidance to mothers (working or not) to pay more attention to the state of their children (knowing the common signs of the presence of a disease). So when there are signs that the child is sick, the disease can immediately treated before it gets worse.