BMS 131 Revision Questions PDF

BMS 131 Revision Carbohydrate: 1- How many molecules produced on hydrolysis of oligosaccharide? a) No molecules produced as it is the simplest form of carbohydrate b) From 3-10 molecules c) More than 10 molecules d) Only 2 molecules 2- How many molecules produced on hydrolysis of...

BMS 131 Revision Carbohydrate: 1- How many molecules produced on hydrolysis of oligosaccharide? a) No molecules produced as it is the simplest form of carbohydrate b) From 3-10 molecules c) More than 10 molecules d) Only 2 molecules 2- How many molecules produced on hydrolysis of disaccharide? a) No molecules produced as it is the simplest form of carbohydrate b) From 3-10 molecules c) More than 10 molecules d) Only 2 molecules 3- How many molecules produced on hydrolysis of polysaccharide? a) No molecules produced as it is the simplest form of carbohydrate b) From 3-10 molecules c) More than 10 molecules d) Only 2 molecules 4- How many molecules produced on hydrolysis of monosaccharide? a) No molecules produced as it is the simplest form of carbohydrate b) From 3-10 molecules c) More than 10 molecules d) Only 2 molecules 5- Hexose sugar is a form of monosaccharide. How many carbons in hexoses? a) 3 Carbons b) 4 Carbons c) 5 Carbons d) 6 Carbons 6- Which of the following compound is an example of ketohexose? a) Dihydroxyacetone b) Glucose c) Fructose d) Galactose 7- Which of the following compound is an example of aldohexose? a) Dihydroxyacetone b) Glucose c) Fructose d) Ribose 8- What is enantomer? a) 2 sugars differ in configuration around one carbon b) 2 sugars differ in configuration around two carbons c) Same types of sugar d) Mirror image sugar 9- Which of the following are epimers to each other? a) Glucose and fructose b) Glucose and galactose c) Glucose and ribose d) Glucose and glyceraldehydes 10- What is epimer? a) 2 sugars differ in configuration around one carbon b) 2 sugars differ in configuration around two carbons c) Same types of sugar d) Mirror image sugar 11- Glucuronic acid obtained by: a) Oxidation of glucose b) Oxidation of galactose c) Reduction of glucose d) Reduction of galactose 12- Mannitol obtained by: a) Oxidation of mannose b) Oxidation of galactose c) Reduction of mannose d) Reduction of galactose 13- Glucosamine is an sugar derivative obtaind by: a) Substitution of OH of C1 of glucose by amino group b) Substitution of OH of C2 of glucose by amino group c) Substitution of OH of C3 of glucose by amino group d) Substitution of OH of C4 of glucose by amino group 14- What is the composition of maltose? a) 2 molecules of glucose b) Glucose + Galactose c) Glucose + Fructose d) Galactose + Galactose 15- What is the composition of lactose? a) 2 molecules of glucose b) Glucose + Galactose c) Glucose + Fructose d) Galactose + Galactose 16- What is the composition of sucrose? a) 2 molecules of glucose b) Glucose + Galactose c) Glucose + Fructose d) Galactose + Galactose 17- Explain why sucrose is a non reducing sugar? a) As both anomeric carbons are involved in linkage b) As it has free carbonyl carbon c) As it has a glycosidic linkage d) As it can by hydrolysed 18- What is the cause of lactose intolerance? a) Deficiency of lactose b) Deficiency of lactase enzyme c) Inability to digest sucrose d) Inability to digest maltose 19- Homopolysaccharide when hydrolysed it will give: a) More than 10 molecules of same type of monosaccharide b) More than 10 molecules of different types of monosaccharide c) 3-10 molecules of same type of monosaccharide d) 3-10 molecules of different types of monosaccharide 20- Starch contain 2 chains which are known as: a) Amylose and cellulose b) Amylopectin and cellulose c) Amylose and amylopectine d) Dextrins 21- Amylopectin differ from amylase chain by being? a) Contains 1,4 glycosidic bond b) Contains 1,6 glycosidic bond at branch point c) Contains glucose and fructose d) Contains glucose and galactose 22- Glycogen is the storage form of: a) Lipid in animal b) Carbohydrate in plant  c) Lipid in plants d) Carbohydrate in animal 23- Why cellulose cannot be hydrolysed in human? a) As it contains α glycosidic bond b) As it contains β glycosidic bond c) As it contains δ glycosidic bond d) As it contains ω glycosidic bond 24- Cellulose is formed of: a) Glucose units b) Galactose units c) Fructose units d) Mixture of glucose and frunctosamine units 25- Binding of glycosaminoglycan to a protein core produce which of the following a) Glycoprotein b) Proteoglycan c) Starch d) Glycogen 26- Which of the following glycosaminoglycan is sulphate free? a) Chondrotin sulphate b) Hayalouronic acid c) Heparan sulphate d) Dermatan sulphate 27- Explain glycosaminoglycan act as shock absorbent? a) As the are non polar so exclude water from the surrounding b) As they are polar, so attract water and expand c) As they are non digestible d) As they contain glycosidic linkage 28- Heparine is one of the glycosaminoglycan compounds, what is the main function of heparin a) Act as shock absorbent b) Act as anticoagulant c) Act as cell adhesion molecule d) Act as lubricant 29- What is the difference between proteoglycan and glycoprotein a) Proteoglycan contain more protein than carbohydrate b) Glycoproteins contain more carbohydrate than protein c) Proteoglycan contain more carbohydrate than protein d) Glycoprotein contain uronic acid and repeated structure 30- Mention cause of Mucopolysachradoses? a) Deficiency of lysosomal enzymes required for degradation of glycosaminoglycan b) Deficiency of lysosomal enzymes required for degradation of phospholipid c) Deficiency of lysosomal enzymes required for degradation of proteins d) Deficiency of lactase enzyme Proteins: 1- Define asymmetric carbon atoms? a) Carbon attached to 2 different group of atoms b) Carbon attached to 3 different group of atoms c) Carbon attached to 4 different group of atoms d) Carbon attached to 4 similar group of atoms 2- Which of the following amino acids does not contains asymmetric atom? a) Valin b) Tyrosine c) Glycine d) Alanine 3- Which of the following is the smallest and simplest amino acid found in protein a) Valin b) Tyrosine c) Glycine d) Alanine 4- Which of the following is an example of imino acid a) Valin b) Tyrosine c) Glycine d) Proline 5- What is the difference between D and L form of amino acids? a) The carboxyl group attached to alpha carbon is on the right in D form b) The carboxyl group attached to alpha carbon is on the left in D form c) The amino group attached to alpha carbon is on the right in D form d) The amino group attached to alpha carbon is on the left in D form 6- Which of the following pair of amino acids are non polar a) Glutamic- Histidine b) Lysin-Aspartic c) Glycine-Valine d) Argnine- glutamic 7- Which of the following pairs of amino acids tend to be on the surface of the protein a) Glutamic- Histidine b) Leucine-Isoleucine c) Glycine-Valine d) Phenylalanine- Tryptophan 8- Which of the following pairs of amino acids tend to be on the interior of the protein a) Glutamic- Histidine b) Lysin-Aspartic c) Glycine-Valine d) Argnine- glutamic 9- Which of the following pair of amino acids are polar uncharged a) Glutamic- Histidine b) Lysin-Aspartic c) Aspargin-Glutamine d) Argnine- glutamic 10- Define essential amino acids? a) These are amino acids essential for growth and life b) These are amino acids which can be synthesized in the body c) These are amino acids which cannot be synthesized in the body and must taken in diet d) These are amino acids which cannot be synthesized in the body and not essential in diet 11- Which of the following is an essential amino acid? a) Alanine b) Valine c) Glutamic acid d) Glutamine 12- Which of the following is a non essential amino acid? a) Valine b)Leucine c) Glutamic acid d) Tryptophan 13- Non essential amino acids characterized by being: a) Not essential in diet b) Not essential for growth c) Must be supplied in diet d) Can be synthesized in body in quantities not sufficient for body need 14- Non essential amino acid are not essential in: a) Protein synthesis b) Body function c) Diet d) Body needs 15- Define peptides? a) Are compounds formed of only one amino acid b) Are compounds formed of 2 or more amino acids linked together by glycosidic bond c) Are compounds formed of 2 or more amino acids linked together by peptide bond d) Are compounds formed of 2 or more amino acids linked together by ester bond 16- How many peptide bonds present in tetrapeptide? a) 2 Peptide bonds b) 3 Peptide bonds c) 4 Peptide bonds d) 5 Peptide bonds 17- How many amino acids present in tetrapeptide? a) One amino acid b) 2 Amino acids c) 3 Amino acids d) 4 Amino acids 18- Which type of bond in protein which is resistant to denaturation? a) Peptide bond b) Electrostatic bond c) Hydrogen bond d) Disulfide bond 19- How does peptide bond can be hydrolysed? a) By minor heating b) By cooling c) By peptidase enzyme d) By UV irradiation 20- What is the composition of glutathione? a) Glutamic-Cystiene-Valine b) Glutamic-valine-Glycine c) Glutamic-Cystiene-Glycine d) Glutamic-Proline-Valine 21- Which of the following is considered as function of glutathione? a) An antioxidant compound b) Enter in synthesis of collagen c) Has anticoagulant activity d) Act as lubricant in joints 22- Which of the following is a covalent bond found in protein? a) Electrostatic bond b) Hydrogen bond c) Disulfide bond d) Hydrophobic interaction 23- Which of the following bonds stabilize potein primary structure? a) Electrostatic bond b) Hydrogen bond c) Peptide bond d) Hydrophobic interaction 24- Define primary order of protein? a) It is a description of amino acids in polypeptide chain b) It is Packed structure of polypeptide chain c) It is local folding of polypeptide chain d) It is Description of shape of protein 25- Define tertiary order of protein? a) It is a description of three dimension structure of protein b) It is a description of amino acids in polypeptide chain c) It is local folding of polypeptide chain d) It is Description of shape of protein 26- Which type of the following bond spared in denaturation? a) Disulfide bond b) Peptide bond c) Electrostatic bond d) Hydrogen bond 27- Antibody is regarded as which of the following type of protein? a) Structural protein b) Defense protein c) Transport protein  d) Catalytic protein 28- Define denaturation of protein? a) Loss of amino acids from protein b) Loss of native nature of protein c) Loss of primary structure of protein d) Loss of peptide bond from protein 29- - Which of the following amino acids can be dissolved in water? a) Glycine b) Leucine c) Glutamic d) Proline 30- Which of the following is a semi-essential amino acid? a) Proline b) Glutamine c) Histidine d) Threonine Enzymes: 1- Define catalyst? a) Chemical substance which speed up rate of reaction and undergoes change in its structure b) Chemical substance which speed up rate of reaction without being itself changed c) Chemical substance which decreases rate of reaction and undergoes change in its structure d) Chemical substance which decreases rate of reaction without being itself changed 2- Which of the following is a character of enzymes? a) All enzymes are protein b) The enzymes are non specific c) Enzymes are not changed chemically by the end of the reaction d) All enzymes require coenzymes 3- What is apoenzyme? a) It is the co factor attached to enzyme b) It is the protein part of holoenzyme c) It is the non protein part of the enzyme d) It is the [protein part + cofactors 4- What is holoenzyme? a) It is the co factor attached to enzyme b) It is the protein part of holoenzyme c) It is the non protein part of the enzyme d) It is the [protein part of the enzyme + cofactors 5- Mention name of coenzyme which is tightly bound to the enzyme?  a) Prosthetic group b) Cosubstrate c) Holoenzyme d) Apoenzyme 6- Mention name of coenzyme which is loosely bound to the enzyme? a) Prosthetic group b) Cosubstrate c) Holoenzyme d) Apoenzyme 7- Which enzymes included in oxidoreductase class of enzymes? a) Enzymes which catalyze transfer of electron or oxygen atom b) Enzymes which catalyze transfer chemical group rather than hydrogen or oxygen c) Enzymes which catalyze ligation of two substrate d) Enzymes which catalyze splitting of substrate without adding water e) What is the name of enzymes which catalyze transfer chemical group rather than hydrogen or oxygen? a) Oxidoreductase b) Transferases c) Ligases d) Hydrolyases 8- What is the name of enzymes which split substrate without adding water? a) Oxidoreductase b) Transferases c) Lyases d) Hydrolases 9- What is the name of enzymes which split substrate by adding water? a) Oxidoreductase b) Transferases c) Lyases d) Hydrolases 10- What is the class of enzymes which catalyze ligation of two substrate together? a) Oxidoreductase b) Transferases c) Ligases d) Hydrolyases 11- What is the name of enzymes which catalyze a structural or geometric change in substrate? a) Oxidoreductase b) Isomerase c) Ligases d) Hydrolyases 12- Define energy of activation? a) Energy required to raise energy level of reactant from ground state to transition state b) Energy required to raise energy level of reactant from transition state to ground state c) Energy required to change shape of active site d) Energy required to denaturate the enzyme 13- What is the transition state? a) It is the point at which enzyme change its shape b) It is the state at which enzyme is stable c) It is the state at which reaction events can occur d) It is the ground energy state energy of reactants 14- Explain how do enzymes speed up rate of reactions? a) By elevating energy barrier b) By lowering free energy of activation c) By stabilizing ground state energy of reactants d) By distortion of shape of active site 15- What is the active site? a) Pocket on enzyme for binding substrate and catalysis of reaction b) Pocket on enzyme which bind to inhibitors and slow down the reaction c) Pocket on substrate facilitate its binding to enzyme d) Pocket on cofactors which facilitate its binding to enzymes 16- Explain the enzyme is specific to its substrate? a) As the substrate fits its active site like lock and key b) As the substrate can induce denaturation of enzyme c) As the cofactors can induce change in enzyme shape d) As the enzyme is specific for the transition state 17- Define optimum temperature? a) Temperature at which enzyme work maximum b) Temperature at which enzyme is denaturated c) Temperature at which the reaction rate is at its lowest value d) Temperature at which substrate is at its ground state 18- What is the optimum temperature of most of enzymes in human body? a) 40 C° b) 37 C° c) 30 C° d) 50 C° 19- Beyond the optimum temperature, what happen to velocity of reaction? a) Increases b) Decreases c) Not changed d) Has no relation to velocity of reaction 20- Define optimum pH? a) It is the pH at which enzyme work maximum b) It is the pH at which enzyme is denaturated c) It is the pH at which the reaction rate is at its lowest value d) It is the pH at which substrate is at its ground state 21- What is the effect of extreme pH on velocity of reaction? a) Increases velocity of reaction b) Decreases velocity of reactions c) Does not affect velocity of reaction d) Increases velocity of reaction then the velocity become stationary 22- Which of the following enzymes has optimum pH of 1-2? a) Trypsin b) Pepsin c) Salivry mylase d) Pancreatic amylase 23- What is the relationship between enzyme concentration and velocity of reaction? a) There is an inverse relationship between them b) There is a direct relationship between them c) There is no relationship between them d) There is a biphasic relationship between them 24- At Vmax of enzyme catalysed reaction, what is the effect of added substrate? a) It increases the velocity of reaction b) It decreases the velocity of reaction c) It does not affect velocity of reaction d) It increases velocity of reaction, followed by decreasing it 25- Define Km? a) Substrate concentration that produce maximum velocity of reaction b) Substrate concentration that produce half maximum velocity of reaction c) Enzyme concentration that produce maximum velocity of reaction d) Enzyme concentration that produce half maximum velocity of reaction 26- What is the effect of competitive inhibitors on enzyme kinetics? a) It increases Km while Vmax unchanged b) It increases Km and Vmax c) It increases Vmax while Km unchnged d) It has no effect on either Km or Vmax 27- Which of the following statement best describes competitive inhibitors? a) It has no structural similarity with the substrate b) It increases Vmax while Km unchanged c) It has structural similarity with the substrate d) It decreases Vmax while Km un changed 28- What is the effect of competitive inhibitors on both Km and Vmax? a) It increases Km while Vmax unchanged b) It decreases Km while vmax un changed c) It decrease Vmax while Km unchanged d) It increases Vmax while Km unchanged 29- What is the effect of non competitive inhibitors on both Km and Vmax? a) It increases Km while Vmax unchanged b) It decreases Km while vmax un changed c) It decrease Vmax while Km unchanged d) It increases Vmax while Km unchanged 30- What is the effect of non competitive inhibitors on enzyme kinetics? a) It decreases Vmax while Km unchanged b) It increases Km and Vmax c) It increases Vmax while Km unchnged d) It has no effect on either Km or Vmax 31- Which of the following statement best describes non competitive inhibitors? a) It has no structural similarity with the substrate b) It increases Vmax while Km unchanged c) It has structural similarity with the substrate d) It decreases both Vmax and Km 32- Which of the following statements best describes enzyme sucide? a) The inhibitor is loosely bound to the enzyme b) The inhibition is reversible c) The inhibitors is covalently bound to the enzyme d) The inhibition can be reverted by increasing substrate cocentartion? 33- Define enzyme induction? a) Increases amount of enzyme b) Decreases amount of enzyme c) Increases amount of substrate d) Decreases amount of substrate 34- Define enzyme represion?  a) Increases amount of enzyme b) Decreases amount of enzyme c) Increases amount of substrate d) Decreases amount of substrate 35- What is allosteric site? a) It is the active site b) Site rather than active site c) Site for binding cofactors d) Site for binding of inhibitors 36- What is the effect of binding of modifier to allosteric site? a) It induces conformational change in substrate b) It induces conformational change in active site c) It induces conformational change in cofactors d) It has no effect on shape of active site 37- What is the effect of covalent modification of enzymes? a) It increases rate of synthesis of enzymes b) It modifies activity of enzymes c) It affect rate of degradation of enzymes d) It decreases rate of synthesis of enzymes 38- In covalent modification of enzymes, phosphate usalyy add to which pairs of amino acids? a) Cystine-Methionine b) Glutamic-Glutamine c) Serine- Therionine d) Tyrosine- Phenylalanine 39- What is effect of covalent modification on enzyme activity? a) It increases enzyme activity b) It decreases enzyme activity c) It may increase or decrease enzyme activity d) It does not affect enzyme activity 40- Define zymogen? a) It is RNA with catalytic activity b) It is an inactive form of the enzyme c) It is active form of the enzyme d) It is the non protein part of an enzyme 41- Which of the following statement best describes isoenzymes? a) It is multiple form of the same enzyme b) It catalyze different reactions c) They cannot be separated from each other d) They are enzymes derived from the same organs 42- Which of the following isoenzyme of creatine kinase (CK) found in the heart? a) CK BB b) CK MM c) CK MB d) CK NM 43- Which of the following isoenzyme of creatine kinase (CK) found in the muscle? a) CK BB b) CK MM c) CK MB d) CK NM 44- Which of the following isoenzyme of creatine kinase (CK) found in the brain? a) CK BB b) CK MM c) CK MB d) CK NM Lipid: 1. Which of the following is a component of the inner core of lipoproteins? a. Free cholesterol b. Phospholipids c. Apoproteins d. Cholesterol ester 2. Lipids are insoluble in ……………. a. Water b. Benzene c. Ether d. Chloroform 3. Chylomicrons are formed in the …………… a. Liver b. Pancreas c. Kidney d. Small intestine 4. Which of the following is a fatty acid that contains 16 carbons with no double bond? a. Oleic b. Stearic  c. Palmitic d. Linoleic 5. Which of the following is a simple lipid? a. Cholesterol b. Lipoprotein c. Glycoprotein d. TAG 6. Each fatty acid has two terminals that contain …………. a. (COOH) and (OH) b. (OH) and (CH3) c. (NH3) and (COOH) d. (COOH) and (CH3) 7. Which of the following lipoproteins contains apo A 1? a. HDL b. LDL] c. VLDL d. Chylomicrons 8. Cholesterol contains ………carbon atoms with an (OH) group at carbon 3 that is mainly esterified with…………… a. 8, amino acid b. 27, fatty acid c. 20, starch d. 15, fatty acid 9. How many fatty acids does each TAG contain? a. 2 b. 3 c. 5 d. 8 10. Which of the following is a bad lipoprotein? a. HDL b. LDL c. VLDL d. Chylomicrons 11. Vitamin D3 and steroid hormones are synthesized from ……………… a. Cholesterol b. Sucrose c. Fructose d. Collagen 12. Which of the following lipoproteins contains apo B 48? a. HDL b. LDL] c. VLDL d. Chylomicrons 13. Which of the following is a complex lipid? a. Cholesterol b. Fatty acid c. TAG d. Phospholipid 14. Arachidonic acid contains …………. carbon atoms and ……. double bonds. a. 16, 2 b. 18, 1 c. 20, 4 d. 24, 3 15. What is the storage form of fatty acids? a. Cholesterol b. Fatty acid c. TAG d. Phospholipid 16. VLDL are synthesised in the ………… a. Liver b. Heart c. Kidney d. Brain 17- Which of the following lipoprotein transport endogenous synthesized TAG? a) Chylomicron b) VLDL c) LDL d) HDL 18- Which of the following lipoprotein transport dietary TAG? a) Chylomicron b) VLDL c) LDL d) HDL 19- Which of the following lipoprotein transport cholesterol to tissue? a) Chylomicron b) VLDL c) LDL d) HDL 19- Which of the following lipoprotein transport excess cholesterol from tissue? a) Chylomicron b) VLDL c) LDL d) HDL 20- Which of the following lipoproteins contains Apo B100 a) Chylomicron b) VLDL c) LDL d) HDL 21- Define amphipathic character? a) The compound carries positive and negative charged pole b) The compound carries two negatively charhed poles c) The compounds has both hydrophilic pole and hydrophobic pole d) The compounds carries two positively charged pole 22- Which of the following fatty acid belongs to ω3 family? a) Oleic b) Palmitic c) Arachidonic d) Linolenic 23- Which of the following is an essential fatty acid? a) Palmitic b) Oleic c) Linoleic d) Stearic 24- This structure formula (20:4, Δ5,8,11,14,) represents which of the following fatty acids? a) Oleic b) Palmitic c) Arachidonic d) Linolenic 25- Explain why linolenic is an essential fatty acid? a) As it is saturated fatty acid b) As the body lack the enzymes required for its synthesis c) As it is ω 9 fatty acid d) As it is ω8 fatty acid 26- What is the hydrolytic product of phosphatidic acid? a) Glycerol + one fatty acid + Phosphate b) Glycerol + 2 fatty acids + Phosphate c) Glycerol+ one fatty acid + serine d) Glycerol +2 fatty acids + choline 27- What is the hydrolytic product of lecithin? a) Glycerol + one fatty acid + Phosphate b) Glycerol + 2 fatty acids + Phosphate c) Glycerol+ one fatty acid + serine d) Glycerol + 2 fatty acids + + phosphate + choline 28- What is the hydrolytic product of phospahtidyl serine acid? a) Glycerol + one fatty acid + Phosphate b) Glycerol + 2 fatty acids + Phosphate+ serine c) Glycerol+ one fatty acid + + phosphate + serine d) Glycerol + 2 fatty acids + + phosphate + choline 29- What is the character of glycerophospholipid? a) Common constituent of cellular cell membrane b) Common constituent of membranous sheet of nerves c) Precursor of vitamin D d) Precursor of steroid hormone 30- What is the character of sphigophospholipid? a) Common constituent of cellular cell membrane b) Common constituent of membranous sheet of nerves c) Precursor of vitamin D d) Precursor of steroid hormone 31- What is the storage form of cholesterol? a) Glycogen b) Triacyl glycerol (TAG) c) Cholesterol ester d) Sphingomyeline s  32- In glycerophospholipid, at which couple of carbons fatty acids usually attached? a) C1 and C2 b) C1 and C3 c) C2 and C3 d) C2 nd C4 33- In glycerophospholipid, carbon phosphate group usually attached? a) C1 of glycerol b) C2 of glycerol c) C3 of glycerol d) C4 of glycerol 34- Which of the following compounds are amphipathic a) Cholesterol b) Triacyl glycerol (TAG) c) Cholesterol ester d) Glactose 35- Which of the following compounds are derived of cholesterol? a) Linoleic acid b) Bile acids and salts c) HDL d) LDL 36- Which of the following lipoproteins act as scavenger for cholesterol? a) Chylomicron b) VLDL c) LDL d) HDL 37- Elevation of which of the following lipoproteins is protective against dyslipidemia and atherosclerosis? a) Chylomicron b) VLDL c) LDL d) HDL Short essay questions: 1- Compare and contrast between starch and glycogen 2- Define enantomer 3- Explain why cellulose prevent constipation 4- Explain why enzyme is specific to its substrate 5- Compare and contrast between functional and non functional plasma enzymes? 6- Enumerate 4 charcteria of non competitive enzyme inhibitors 7- Why leucine is regarded as essential amino acid? 8- Define denaturation and enumerate 2 effects of it on protein? 9- Define amphipathic character and give 2 examples? 10- Mention structure and 2 functions of glutathione 11- Define enzyme repression 12- Enumerate 2 essential fatty acids? 13- Enumerate 2 functions of cholesterol? 14- How to cholesterol transported in blood? 15- Mention function of chylomicron? 16- Mention function of VLDL? 17- Mention function of LDL 18- Mention function of HDL