01071180028 Cindy Clarissa Thandy

BIOCHEM

Functions Chemistry bonds

1. Cholesterol
Molecule Bond Monomer
- react with fatty acid = esters (less soluble,
can be stored) Polysaccharides 1,4 and 1,6 Monosaccharides
- #lipoprotein in blood glycosidic
bond
- maintain membrane fluidity
2. Bile salt Protein peptide, Amino acids
hydrogen,
- emulsify lipid ionice,
3. Lung surfactant disulphide,
- decrease surface tension to maintain hydrophobic
interaction,
alveolar space VDWF
4. Haemoglobin
Lipid Esters Triacylglycerol
- transport O2 by binding to it from lungs to
tissues Nucleic acid Phospodiester nucelotide
5. Buffer system
- maintain pH balance in body Precursors
- keep venous blood only 0.01-0.03 more 1. Bile salt synthesis : cholesterol
acidic than arterial 7.40 vs 7.43 2. Haem synthesis : glycine
6. Metabolism of Xenobiotic 3. Pepsin : pepsinogen (inactive precursor)
- increase water solubility of xenobiotics and
facilitate excretion from body Meanings
- PHASE I: convert inactive xenobiotics to 1. Structure level of protein + examples
active biological compounds (or kebalik) - primary: linear (peptide bond)
- PHASE II: conjugation reaction preparing - #
xenobiotics for excretion - secondary: alpha-helix or beta-pleated
sheets (peptide and H bonds)
Definitions - #myoglobins, antibodies, T cell receptor
1. D and L isomer in monosaccharide and - tertiary: 3D form (ionic, disulphide, H,
amino acid peptide bonds, hydrophobic interaction,
- D: hydroxyl group on the right VDWF)
- L: hydroxyl group on the left - #
- depends on chiral C furthest from carbonyl - quaternary: >1 polypeptide chain (non
2. Cis and trans isomer in unsaturated fatty covalent interaction)
acid - #globular - enzymes
- cis: functional groups are on the same side - #haemoglobin
- polar, flexible, mobile, recognized by - #fibrosis - collagen
body 2. Chloride shift
- trans: functional groups on the opposing - exchange of chloride and bicarbonate
sides (HCO3) across er ythrocyte sur face
membrane to maintain electrical neutrality
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Mechanism of compensation in acid base Main location of energy synthesis in cell
imbalance Mitochondria
- buffers: bicarbonate and oxyhemoglobin to - glycolysis: cytosol
keep pH at 7.37-7.43 - Krebs:
- act in conjunction with mechanism in - ETC:
kidneys for excreting protons as - Oxidative phosporilation
- in lungs to exhale CO2 to maintain pH with
normal range Main oran having roles in
1. Cholesterol synthesis = LIVER
Types of acid base inbalance in certain 2. Urea cycle = cytosol & mitochondria
disease matrix of the liver
- metabolic acidosis 3. Absorption of most nutrition consumed =
- metabolic alkalosis SMALL INTESTINE
- respiratory acidosis 4. Absorption of most water from nutrition
- increase in H2CO3 consumed = LARGE INTESTINE
- happen in impaired respiration and
morphine poisoning Vitamins required in synthesis of haem
- respiratory alkalosis B5
- drop in H2CO3
Structure of DNA double helix
Main organs role in acid base balance - C and G = 3 bonds
kidney and lungs - A and T = 2 bonds
- sugar phosphate backbone
End products - deoxyribose
1. Purine and pyrimidine catabolism - phospate
- purine: uric acid - hydrophobic backs stack together and
- hypoxanthine - xanthine - uric acid interact between 2 strands
- pyrimidine
- urasil (U) and cytosine (C) = beta-alanine Examples
- thymine (T) = beta-isobutyrate 1. Monosaccharides
2. Haem catabolism: bilirubin - triose: glyceraldehyde
3. Protein carabolism: amino acid - tetrose: erythose
- pentose: ribose
Characteristics of porphyrin - hexose: glucose, sucrose, fructose,
1. colored substance mannose
2. red fluorescence - heptose: sedoheptulose
3. soret band (absorption curve in UV region 2. Polysaccharides
400nm) - starch (glucosan)
- glycogen (glucosan)
Storage structure of carbohydrate in body - amylum (glucosan)
Starch, glycogen - inulin (fructosan)
- glycosaminoglycan (mixed)
Storage structure of fat in body 3. Aldose and ketose
metabolic fuel - aldose: glyceraldehyde, glycoaldehyde,
erythrose, threose, ribose, glucose,
mannose, galactose
01071180028 Cindy Clarissa Thandy
- ketose: fructose, erythrulose, 9. Amino acid containing sulfur
dihydroxyacetone methionine and cysteine
4. Epimer pairs 10. Endopeptidase, exopeptidase, protease
- beda 1 posisi OH having autocatalytic characteristics
- D-glucose dan D-mannose - Endopeptidase: pepsin, trypsin,
5. Monomers of chymotripsin, elastase, glutamyl,
- protein: amino acid thermolysim, neprilysin
- glycogen: glucose - Exopeptidase: carboxypeptidase,
- starch: glucose aminopeptidase, dipeptidase
6. Essential and non essential amino acids - protease: trypsin, pepsin
Essential Non-essential 11. Strong and weak acid bases

Methionine Tyrosine

Phenylalanine Glycine

Threonine Alanine

Tryptophan Cystine

Valine Serine

Isoleucine Aspartic

Leucine Asparagine

Lycine Glutamic

Histidine Glutamine 12. Substance that undergoes enterohepatic

circulation
Arginine Proline
- biliary acid
7. Essential fatty acids - bilirubin
- LINOLEIC - drugs
- LINOLENIC LIVER TO BILE
- ARACHIDONIC
omega 3 fatty acids — menghasilkan
golongan eksonaoat #prostagladin
8. Steroid, saturated fatty acid, unsaturated
fatty acid

Steroid Saturated Unsaturated

Cholesterol Propanoic Eicosanoids

(prostagladins,
thromboxans)

Sex hormones butyrics Palmitoleic

Adrenocorticol Lauric Oleic 13. Iron porphyrin

hormone - haem (haemoglobin, myoglobin,
Myristic Linoleic c y t o c h ro m e , c a t a l a s e , p e ro x i d a s e ,
tryptophan, pyrolase)
Palmitic Andarachidonic - in plants: Mg
Stearic - in human: Fe
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14. Anabolic and catabolic pathways
- anabolic: gluconeogenesis, glycogenesis
- catabolic: glycolysis, Krebs, oxidative
phosporylation
15. Buffer system in the blood
- plasma protein
- haemoglobin
- oxyhemoglobin
- bicarbonate
- inorganic phosphate
16. Protease produced by pancreas, stomach,
and small intestine
- pancreas:
- trypsin
- chymotrypsin
- elastase
- carboxypeptidase
- stomach:
- pepsin
- small intestine
- dipeptidase
- amino-peptidase
17. Enzymes produced by pancreas and
small intestine
- pancreas: lipase
- small intestine: amylase