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Introduction to Biochemistry
Basic Principles and Importance of Biochemistry in relation to Other Sciences
Chemical Basis of Life
Content
1. Chemical composition and organization of a cell: Carbohydrates, Lipids, Amino acids and Proteins, Nucleic acids: DNA and RNA
2. Chemical composition and organization of membranes
Objectives
Level 1
1. List the normal chemical compositions of a cell.
2. List cellular organelles and state their metabolic functions.
3. Classify biologically important sugars and state their important features.
4. State the reactions of monosaccharides.
5. State the component of dietary disaccharides, starch, glycogen, heteroglycans and mucopolysaccharides.
6. Describe briefly the biomedical importance of disaccharides and complex sugars.
7. Classify lipids according to their basic structure.
8. Classify fatty acids according to their structures.
9. Explain the differences between saturated and unsaturated fatty acids.
10. Classify compound lipids according to their compositions.
11. State the components of phospholipids and their biochemical significance.
12. State the components of glycolipids and their biochemical significance.
13. Differentiate nucleic acids and nucleotides.
14. List the components of deoxyribonucleotide and ribonucleotide.
15. Describe the properties of nucleotides.
16. Describe the general structures of DNA and RNA.
17. Classify amino acids based on side chains, structures and functions.
18. State the important reactions of amino and carboxy groups of amino acids.
19. Explain peptide bond formation with diagram.
20. Describe the four orders of protein structure.
21. Classify proteins according to their structures and functions.
22. Enumerate important tissue proteins and state their roles.
23. List the structures of plasma membrane and state the role of each molecule.
24. List the components of biomembrane.
Level 2
1. Explain some important properties of sugars.
2. Explain important physical properties of triacylglycerol and rancidity.
3. Explain precipitation of protein and its clinical significance.
4. State the principle of quantitative estimation of protein.
Molecular Biology Content
• Organization of genomes and chromosomes of prokaryotes & eukaryote
• Central Dogma of Molecular Biology
• Structures and functions of nucleic acids (DNA & RNAs)
• Functional gene
• Genetic code and its importance
• Biomedical aspect of genomic stability and Mutation
• Genetic diseases
• Gene expression: Transcription and Translation (Protein Synthesis)
• Regulation of gene expression
• Cell cycle and apoptosis
• DNA replication, Reverse transcription
• DNA damage and repair
• Oncogenes and tumour biomarkers
• Recombinant DNA technology, Cloning, PCR
• Human genome project, Gene therapy and Stem cell therapy
Objectives
Level 1
• Outline the flow of genetic information or central dogma of molecular biology.
• Describe the structure and functions of DNA and RNA.
• Describe the organization of genome and chromosomes.
• Describe a functional gene.
• Define gene expression.
• Describe the basic concept of gene expression.
• Describe the genetic code and its characteristic features.
• Describe the process of transcription.
• Describe the role of transcriptional factors in eukaryotic transcription.
• Outline the mechanisms of post-transcriptional modifications of RNAs.
• State the importance of mRNA splicing and diseases.
• State the similarity and dissimilarity of replication and transcription.
• Describe the process of translation.
• Describe the importance of nutrition, hormones, growth factors and viral infection in protein synthesis.
• Outline the mechanisms of post-translational modification of proteins.
• State the similarity and dissimilarity of transcription and translation.
• Outline the regulatory mechanisms of gene expression in eukaryote.
• Define genomic stability.
• Describe cell cycle and its regulation.
• Describe the process of DNA replication and reverse transcription.
• Describe the importance of reverse transcription in medicine and research.
• Stale the common causes, mechanisms and types of DNA damage.
• Describe the mechanisms of DNA repair and their significance.
• What is apoptosis? Outline the molecular mechanisms of apoptosis.
• State the importance of apoptosis for genomic stability.
• List the types of mutations.
• Describe gene mutation and its importance.
• Define proto-oncogene, tumour suppressor gene and oncogene.
• What is tumour marker? State the clinically useful tumor markers.
• Define recombinant DNA and recombinant DNA technology.
• List the common techniques used in recombinant DNA technology.
Level 2
• Define genetic diseases.
• Name the common genetic diseases.
• State the differences between inherited diseases and congenital diseases according to molecular basis.
• State the importance of restriction fragment length polymorphism (RFLP).
• State the different types of gene library.
• List different hybridization techniques.
• State the purpose of hybridization techniques.
• Describe the molecular mechanisms that convert normal genes to oncogenes.
• Describe the steps of PCR, RT-PCR and real-time PCR and their roles in medicine.
• Describe the role of recombinant DNA technology in medicine.
• Define recombinant DNA and recombinant DNA technology.
• List the common techniques used in recombinant DNA technology.
• Describe the steps of PCR, RT-PCR and real-time PCR and their roles in medicine.
• Describe the role of recombinant DNA technology in medicine.
Level 2
• Define genetic diseases.
• Name the common genetic diseases.
• State the differences between inherited diseases and congenital diseases according to molecular basis.
• State the importance of restriction fragment length polymorphism (RFLP).
• State the different types of gene library.
• List different hybridization techniques.
• State the purpose of hybridization techniques.
• Describe the molecular mechanisms that convert normal genes to oncogenes.
Level 3
• State Human Genome Project (HGP).
• State the benefits of HGP.
• State the role of recombinant DNA technology in Forensic Medicine.
• Define 'Pharmacogenomics'.
• What is ‘gene therapy’? Outline the steps involved in gene therapy.
• Define stem cell. What is stem cell research?
• List the different types of stem cell.
• State the roles of the stem cell therapy and gene therapy in medicine.
• State the ethics concerned with HGP, gene therapy and stem cell research.
EnzymologyContent
• Definition, chemical structure and properties of enzyme
• Distribution of enzyme
• Classification of enzyme
• Specificity of enzyme
• Coenzymes, cofactors and abzymes and their functions
• Isoenzyme and its biomedical importance
• Mechanism of enzyme action
• Factors affecting the velocity of enzyme-catalyzed reactions
• Enzyme inhibition
• Biomedical importance of enzyme inhibition
• Regulation of enzyme activity
• Medical aspects of enzymology
Objectives
Level 1
Define:
• Enzyme allosteric enzyme
• Coenzyme abzymes
• Cofactor chaperone
• isoenzyme
State the chemical nature and structure of protein enzyme.
1. Define denaturation and renaturation
2. State the distribution of enzymes in cellular compartments.
3. List the IUBMB classification of enzymes.
4. State the specificity of enzyme for its substrate.
5. List the models that explain the mechanism of action of enzyme.
6. Outline the differences between lock-and-key model and induced-fit model of enzyme specificity.
7. Outline the binding mechanisms of multi-substrate enzyme.
8. Explain the mechanisms of enzyme action.
9. Explain Michaelis-Menton theory.
10. Describe isoenzyme and its importance in clinical medicine.
11. List the factors affecting the velocity of an enzyme-catalyzed reaction.
12. Explain the effects of those factors on enzyme reaction in both physiological and pathological conditions.
13. Explain the mechanisms of enzyme inhibition.
14. Describe the role of enzyme inhibitors in medicine.
15. Describe the role of enzymes in clinical medicine.
16. Explain the mechanisms of enzyme regulation and their importance in metabolism.
17. State the principles of the effects of temperature, pH and inhibitors on the velocity of enzyme-catalyzed reaction.
18. Demonstrate the effects of temperature, pH and inhibitors on the velocity of enzyme-catalyzed reaction.
19. Interpret the effects of temperature, pH and inhibitors on the velocity of enzymecatalyzed reaction on the given data in a problem.
Level 2
• Distinguish different types of inhibitors using Lineweaver-Burk plots.
Level 3
• Describe the principle and usage of enzyme in ELISA.
• Explain the mechanism of enzyme catalysis with molecular basis.
Chemistry of Blood Content
1. Components and functions of blood
2. Hemoglobin structure and functions
3. Normal and abnormal variants of haemoglobin
4. Synthesis and breakdown of Hb and their biomedical importance
5. Plasma proteins and their functions
6. Factors maintaining the plasma protein level
7. Biochemistry of proteins that are involved in immune system: immunoglobulins, complement proteins, cytokines
8. Biochemical mechanism of blood coagulation & anti-clotting, and their importance
Objectives
Level 1
1. Outline the general functions of blood.
2. State the constituents of blood.
3. Describe the biochemistry of blood cells.
4. State the normal haemoglobin levels of Myanmar adult male and female, and the influencing factors.
5. Describe the structure and functions of haemoglobin.
6. List the different types of normal and abnormal haemoglobins.
7. State the formation and importance of HbA1c.
8. Outline the synthesis of haemoglobin.
9. State the chromosomes where globin genes are located.
10. State the conditions arising from abnormal synthesis of heme and globin chains.
11. Differentiate between haemoglobin variants and thalassaemia.
12. Describe the breakdown of haemoglobin or bilirubin metabolism.
13. State the normal bilirubin concentration in plasma.
14. List the different types of hyperbilirubinaemia.
15. State the biochemical basis of neonatal/physiologic jaundice.
16. Explain the differences between conjugated and unconjugated bilirubin and their clinical significance, and state the clinical significance of urinary urobilinogen.
17. Differentiate plasma and serum.
18. List the major fractions of plasma proteins.
19. State the concentrations of different plasma protein fractions and albumin:globulin ratio of a healthy person.
20. State the methods for separation of plasma proteins.
21. State the sources of plasma proteins.
22. Enumerate the functions of plasma proteins.
23. Describe the factors affecting the concentrations of plasma proteins.
24. Describe the functions of different fractions of plasma proteins.
25. List the components of immune system.
26. Define immunoglobulin.
27. State the sources and major types of immunoglobulin.
28. Describe the structures and functions of immunoglobulins.
29. List the coagulation factors with their biochemical functions.
30. Outline the general process of coagulation.
31. Explain the molecular mechanisms of the activation of coagulation factors.
32. State the anti-clotting mechanisms and their importance.
33. Describe fibrinolytic system.
34. State the principle of the determination of haemoglobin.
35. Perform the determination of haemoglobin by Cyanmethaemoglobin method.
36. Interpret the level of haemoglobin by the given data.
37. State the principles of the determinations of total plasma proteins and albumin.
38. Perform the determinations of total and differential plasma proteins concentrations.
39. Interpret the levels of total and differential plasma proteins by the given data.
Level 2
1. State the acute phase proteins.
2. Name the sources of acute phase proteins.
3. State the role of complement proteins and cytokines in immune system.
4. Describe the biochemical abnormalities of coagulation and fibrinolytic mechanisms in disease conditions.
Level 3
1. Describe how abnormal haemoglobins differ from HbA.
2. Explain the development of anaemia in HbS.
3. State the disorders of immunoglobulin synthesis.
4. Describe the relationship between coagulation mechanism and fibrinolytic mechanism.
Chemistry of RespirationContent
1. Gas laws and biochemical aspect of respiration
2. General process of gas transfer
3. Transport of respiratory gases: O2 and CO2
4. Molecular mechanism of oxygen-binding to Hb
5. Oxygen hemoglobin dissociation curve and its significance
6. Factors influencing O2 dissociation: pH, temperature, electrolytes, CO, CO2 &
7. 2,3-BPG
8. Carbon monoxide toxicity
9. Oxygen binding ability of Hb variants (HbF, HbS), methaemoglobin, etc.
10. Myoglobin
11. Clinical applications of blood gas analysis
Objectives
Level 1
1. State the important properties of gases.
2. Explain gas laws.
3. State the compositions of inspired air and expired air.
4. List the factors affecting the diffusion of gases across the alveolar membrane.
5. Define (i) partial pressure, (ii) diffusion capacity of gases.
6. Illustrate and outline the sequence of respiratory gas transport.
7. Describe how oxygen is transported in the blood.
8. Explain the molecular mechanisms of the binding of oxygen and haemoglobin.
9. Describe the importance of haemoglobin structure in gas transport.
10. Draw and describe the oxygen haemoglobin dissociation curve.
11. Explain the significance of the oxygen haemoglobin dissociation curve.
12. List the factors affecting the oxygen haemoglobin dissociation curve.
13. Explain the effects of hydrogen ion concentration, body temperature, partial pressure of CO2, plasma electrolyte concentration on oxygen-binding ability of haemoglobin.
14. Describe the source and general structure of 2,3-BPG.
15. List the factors affecting the concentration of 2,3-BPG in RBC.
16. Describe the role of 2,3-BPG on oxygen-binding of haemoglobin.
17. Compare and contrast haemoglobin and myoglobin.
18. Describe the mechanisms of carbon dioxide transport.
19. Explain the chloride shift phenomenon (including reverse chloride shift) during carbon dioxide transport.
Level 2
1. State the clinical significance of blood substitutes.
2. Describe the effect of CO poisoning on oxygen-binding capacity of haemoglobin.
3. Explain the effects of exercise on oxygen haemoglobin dissociation.
4. Explain the effects of blood pH, body temperature and electrolyte concentration on oxygen haemoglobin dissociation.
Level 3
1. State the clinical significance of methaemoglobin.
2. State the oxygen haemoglobin dissociation in other haemoglobin variants.
3. List the tests performed in blood gas analysis.
4. State the importance of blood gas analysis.
NutritionContent
1. Energy aspect of diet
2. Nutritional importance of dietary carbohydrate, fat and protein
3. Dietary fibres
4. Nitrogen balance
5. Nutritional and biochemical aspect of fat-soluble and water-soluble vitamins
6. Energy-releasing vitamins
7. Antioxidant vitamins
8. Haemopoietic vitamins
9. Anti-vitamins
10. Minerals
11. Compositions of a balanced diet
12. Principles in planning a balanced diet
13. Nutritional and biochemical aspect of genetically modified foods
Objectives
Level 1
1. Define nutrition, nutrients and RDA.
2. State the importance of good nutrition.
3. List the essential nutrients.
4. List the major functions of each nutrient.
5. List the sources of energy in the body.
6. State the proportions of total calories contributed by carbohydrate, fat and protein.
7. State the calorific values of carbohydrate, fat and protein.
8. List dietary carbohydrates and their common sources.
9. Describe the biochemical roles of dietary carbohydrates.
10. State the daily requirement of carbohydrate.
11. State the deficiency state of protein-calorie in children.
12. Name the state of prolonged excessive intake of carbohydrate.
13. Define dietary fibre. State the biochemical roles of dietary fibres.
14. List the sources of animal proteins.
15. List the sources of vegetable proteins.
16. Define and list essential amino acids. State the methods for the measurement of quality of proteins.
17. Define limiting amino acid and state its importance in nutrition.
18. Describe the biochemical roles and state the daily requirement of dietary proteins.
19. State the deficiency state of protein in children.
20. List dietary fats and their sources.
21. Describe the biochemical roles and state the daily requirement of dietary lipids.
22. Define and list essential fatty acids.
23. List cholesterol-rich foods.
24. State the daily requirement of fat.
25. Define energy balance, positive energy balance and negative energy balance. Give examples.
26. Define vitamin.
27. List the classification of vitamins.
28. List fat-soluble vitamins and name the rich sources of each.
29. Describe the biochemical functions and state the daily requirements of fat-soluble vitamins.
30. Name the common clinical conditions caused by deficiency and excess states of fatsoluble vitamins / water-soluble vitamins.
31. List water-soluble vitamins and name the rich sources of each.
32. Describe the biochemical functions and state the daily requirements of watersoluble vitamins.
33. Name the vitamins that are involved in energy production reaction.
34. Describe the role of vitamins in energy production reaction.
35. Describe the coenzyme functions of vitamin B complex.
36. List anti-anemic nutrients.
37. Describe the role of nutrients in prevention of anaemia.
38. Name the anti-oxidant nutrients.
39. Describe the role of nutrients in anti-oxidant action.
40. State the biochemical role of minerals.
41. Define and list the macronutrients / micronutrients.
42. State the total amount, major distribution and biochemical functions of calcium in the body. State the normal blood calcium level.
43. List the common sources of calcium. State the daily requirement of calcium.
44. State the factors that influence the calcium absorption from intestine.
45. List the common sources of iron. State the daily requirements of iron in children, men, women in reproductive age, pregnant and lactating women, and postmenopausal women.
46. State the total amount, the distribution in the body and the different forms of iron.
47. State the normal plasma iron level.
48. Describe the biochemical functions and metabolism of iron.
49. State the factors influencing iron absorption in intestine.
50. Describe the mechanism of the regulation of iron absorption.
51. State the clinical conditions that occur in deficiency or excess state of iron.
52. List the common sources of iodine. 51. State the role of iodine in the body.
53. Name the major clinical conditions of iodine deficiency or excess.
54. List the common sources of zinc.
55. Describe the roles of zinc in the body.
56. Name the common conditions of zinc deficiency.
57. Define ‘balanced diet’. List the components of a balanced diet.
58. State three food group plan.
59. State the principles in planning of a balanced diet.
60. State the principle of body mass index (BMI) (definition, calculation, normal range).
61. Perform the anthropometric measurement of a person.
62. Calculate and interpret the data of BMI, body fat percent and waist:hip ratio of the given subject.
63. Accept the ethics in patient-doctor relationship or subject-researcher relationship by showing the habit of taking informed consent, gentle handling to subjects when experiments are being done.
64. State the normal blood levels of sodium, chloride and potassium.
65. State the sources and biochemical functions of other macrominerals.
66. State the sources, daily requirements, functions and deficiency / excess states of iodine, fluorine, zinc and other trace elements.
67. State the distribution, sources, daily requirement and functions of water in the body.
Level 2
1. Define malnutrition.
2. List the common conditions which can give rise to malnutrition.
3. Explain the role of balanced diet in healthy life style.
4. Define anti-vitamins.
5. State the biochemical mechanisms of anti-vitamins.
6. State the methods for assessing the nutritional status of a community.
Level 3
1. List the nutrients that are required for brain development.
2. Describe the role of nutrients in brain development.
3. List the nutrients that are required for bone formation.
4. Describe the role of nutrients in bone formation.
5. Define GM food.
6. State the nutritional aspect of GM food.
7. Discuss the role of GM food in health.
Digestion and AbsorptionContent
1. Digestion and absorption of carbohydrate and its clinical importance
2. Digestion and absorption of protein and its clinical importance
3. Digestion and absorption of lipid and its clinical importance
4. Digestion and absorption of nucleoprotein
5. Absorption of water and minerals
6. Absorption of vitamins
7. Absorption in large intestine
Objectives
Level 1
1. Define digestion and absorption.
2. List the organs of gastrointestinal tract with their major functions in digestion and absorption.
3. List the sources and different types of dietary carbohydrate.
4. Describe the digestion of carbohydrate in gastrointestinal tract.
5. List the end products of carbohydrate digestion.
6. Describe the absorption of the end products of carbohydrate digestion.
7. List the sources and different types of dietary proteins.
8. Describe the digestion of protein in gastrointestinal tract.
9. Name the proteolytic enzymes present in gastric, pancreatic and intestinal secretions.
10. Outline the activation of zymogens of digestive system.
11. List the end products of protein digestion.
12. Describe the absorption of the end products of protein digestion.
13. List the sources and different types of dietary lipids.
14. Describe the digestion of lipids in the gastrointestinal tract.
15. List the end products of lipid digestion.
16. Describe the absorption of the end products of lipid digestion.
17. Describe the absorption of vitamins, minerals and water in GI tract.
18. Explain the importance of bile salts in fat digestion and absorption.
19. State the biomedical importance of absorption in large intestine.
20. State the principle and perform the determination of gastric acidity.
21. Interpret the gastric function of an individual by the given gastric acidity in a problem.
22. State the principle and perform the determination of pancreatic amylase activity.
23. Interpret the pancreatic function of an individual by the given activity of the enzyme pancreatic amylase in a problem.
24. Describe the digestion and absorption of dietary nucleic acids in GI tract.
Level 2
1. Explain the biochemical basis of diarrhoea due to cholera toxin and lactose intolerance.
2. State the compositions of oral rehydration salt.
3. Explain the biochemical mechanism of oral rehydration salt and laxatives.
4. Describe the biochemical basis of steatorrhoea.
5. State the role of -glutamyl cycle in amino acid absorption.
Level 3
1. Functions of liver
2. Liver function tests and their clinical uses
3. Bile: composition and functions
4. Synthesis and functions of bile salts
5. Biochemical mechanism of gallstone formation
6. Biomedical importance of liver and biliary system
Objectives
Level 1
1. List the major functions of liver.
2. Describe the protective and detoxification functions of liver.
3. Describe the metabolic functions of liver.
4. Describe the biotransformation functions of liver.
5. State the liver function tests according to the major functions of liver.
6. List the constituents of bile.
7. State the differences between hepatic bile and gall bladder bile.
8. Name the primary and secondary bile acids.
9. Outline the bile acid / bile salt formation.
10. Describe the functions of bile and bile salts.
11. Describe the metabolism of bile acids / bile salts.
12. State the principles, and perform and interpret the determinations of urinary bile salts and bile pigments.
Level 2
1. Describe the role of liver in nutrient metabolism.
2. Describe the biochemical changes in the body when liver functions are impaired.
3. Explain the biochemical basis of gallstone formation.
4. Describe cytochrome P450 enzyme system.
Fluid and ElectrolytesContent
1. Body fluid compartments, Distribution of water
2. Factors affecting the total body water
3. Importance of plasma electrolytes
4. Principles of measurement of fluid compartment
5. Functions of water and electrolytes
6. Water balance: daily intake and output of water
7. Regulation of ECF volume and osmolarity
8. Disturbances of sodium and water metabolism: Dehydration, Overhydration
9. Fluid shift
Objectives
Level 1
1. Illustrate body fluid compartments.
2. State the percentage distribution of body fluids in relation to body weight.
3. State the principle for the measurement of body fluid compartments.
4. Name the substances used in the measurement of each body fluid compartment.
5. Calculate the volumes of body fluid compartments by the given weight of an individual.
6. List the compositions of body fluid.
7. State the factors influencing the total body water.
8. Define osmolality and osmolarity.
9. State the normal osmolality of plasma.
10. Name the principal cations and anions of ECF and ICF.
11. State the concentrations of plasma electrolytes of a healthy individual.
12. Describe the functions of water and electrolytes.
13. Describe water balance.
14. List the mechanisms regulating ECF volume and tonicity.
15. Describe the role of ADH, RAA system, ANP and thirst mechanism in the regulation of ECF volume and tonicity.
16. State the principle and perform the determination of physical examination of urine.
17. Interpret the given physical data of a urine sample.
18. Perform and interpret the specific gravity and total solid contents of a given urine sample.
Level 2
1. State the common causes of dehydration and water excess.
2. Explain fluid shift between ECF & ICF with Darrow-Yannet diagrams.
3. Explain the body's response to dehydration and water excess.
Level 3
1. Explain the disturbances of sodium and water metabolism.
2. Describe the fluid and electrolyte status in an uncontrolled diabetes mellitus patient.
Acid-Base Balance
Content
Fundamental concept of acid-base balance
Production of acid and base in the body
Regulation of hydrogen ion concentration
Regulation by buffer mechanism
Respiratory adjustment
Renal adjustment
Acid base disturbances: Metabolic acidosis and alkalosis
Respiratory acidosis and alkalosis
Importance of anion gap in acid-base imbalance
Assessment of acid-base status
Objectives
Level 1
1. Define
a. Acid (e) Buffer
b. Base (f) Buffer capacity
c. pH (g) Acidosis (respiratory and metabolic)
d. pKa (h) Alkalosis (respiratory and metabolic)
1. Recall the Henderson-Hasselbalch equation.
2. State the normal pH values and hydrogen ion concentrations of body fluids.
3. State the hydrogen ion concentrations which correspond to pH values.
4. Describe the sources of hydrogen ions in the body.
5. Describe the sources of alkali in the body.
6. List the mechanisms of pH homeostasis in the body.
7. List buffer pairs of body fluids.
8. State the percentage distribution of buffer pairs in plasma.
9. State the importance of buffer in acid-base balance.
10. Describe the mechanism of buffer action.
11. Describe the roles of
a. HCO3– / H2CO3 buffer pair
b. Deoxyhaemoglobin / Oxyhaemoglobin buffer pair
12. Describe the respiratory adjustments to pH changes.
13. Describe the renal adjustments to pH changes.
14. Define anion gap.
15. State the importance of anion gap.
16. Name five causes of acidosis and alkalosis.
Level 2
1. Explain acid-base disturbances with examples.
2. Describe the regulatory responses of the body in acidosis and alkalosis.
3. Differentiate different types of metabolic acidosis.
Cell Signaling and Biochemistry of Hormones
Content
• Cell signaling
• Signaling mechanisms of special senses
• Signaling mechanisms of growth factors and cytokines
• Second messengers
• General characteristics of hormones
• Biosynthesis and signaling mechanisms of hormones
• hormone (e) cell signaling
• signal transduction (f) target cell
• signaling molecule (g) receptor
• second messenger
• Outline the general characteristics of hormones.
• State the chemical nature of hormones.
• State the classification of hormones.
• Describe the general mechanism of cell signaling.
• State the different types of receptors.
• Describe the mechanisms of different types of receptor.
• List second messengers.
• Explain second messenger concept.
• Describe second messengers.
• Describe G protein.
• Describe the mechanisms of the actions of lipophilic and hydrophilic signaling molecules.
• Name the principle polypeptide, protein and steroid hormones.
• Describe the biosyntheses of thyroid hormones, steroid hormones and catecholamines.
• Describe the biochemistry of insulin, epinephrine and thyroid hormones.
• State the normal blood calcium level.
• List the hormones regulating plasma calcium level.
• Describe the role of calcitriol, parathyroid hormone and calcitonin in calcium homeostasis.
• State the principle and perform the determination of urinary calcium.
• Interpret the presence or absence of calcium in the given urine sample.
Level 2
• Explain the signal transduction of special senses.
• Explain the implication of the process of cell signaling in the following conditions:
(a) Cholera toxin
b. Pertussis toxin
c. Oncogene products, growth factors and their receptors
d. Nitric oxide
e. Receptor blockers 3. Define growth factor.
• State the major differences between growth factor and hormone.
• Name five important growth factors.
• Describe the differences in signaling mechanisms of 1 and 2 adrenergic receptors in response to the same signaling molecule.
Level 3
• Explain the signal transduction of cell communication.
• Correlate the signaling mechanism and gene expression.
Bioenergetics and Biologic Oxidation Content
• Laws of Thermodynamics
• Extraction of chemical energy by a cell
• Mitochondria and energy extraction
• Respiratory chain, Oxidative phosphorylation
• Biomedical importance of inhibitors and uncouples
• Energy rich compounds and their functions
• Biologic oxidation
• Enzymes and coenzyme involved in biologic oxidation
• Reactive oxygen species and oxidative stress of the cell
Objectives
Level 1
Define:
1. Bioenergetics (g) Redox potential
2. Thermodynamics (h) Biologic oxidation
3. Free energy change (i) Oxidation
4. Standard free energy change (j) Reduction
5. Enthalpy (k) Reactive oxygen species
6. Entropy (l) Free radicals
• Explain the nature of exergonic and endergonic reaction.
• State the energy unit.
• List the different types of energy.
• Name the sources of chemical energy.
• Explain why energy is required for human body.
• State the laws of thermodynamics.
• Describe the general mechanism of energy extraction of cells from food.
• Describe respiratory chain and its importance.
• Define oxidative phosphorylation.
• Describe different types of oxidative phosphorylation.
• Name the important inhibitors of oxidative phosphorylation.
• Name the sites where oxidative phosphorylation occur.
• Explain chemiosmotic hypothesis in oxidative phosphorylation.
• Define uncouplers and state their importance in energy production.
• List common exogenous and endogenous uncouplers and state their mechanisms.
• Describe the role of respiratory chain in energy capture.
• Outline the structure and functions of mitochondria.
• Enumerate the mitochondrial transporter systems.
• Define energy rich compounds.
• List energy rich compounds in the body.
• State the physiological and biochemical importance of adenosine triphosphate.
• State the biochemical functions of energy rich compounds.
• List the enzymes and coenzymes involved in biologic oxidation.
• State their roles in cellular metabolism.
• List reactive oxygen species.
• List anti-oxidant mechanisms in the body.
Level 2
1. Describe the regulation of oxidative phosphorylation.
2. Describe the roles of microsomal and mitochondrial cytochrome P450 systems.
3. Describe oxygen toxicity.
4. Outline the generation mechanisms of reactive oxygen species in the body.
5. Describe the role of reactive oxygen species in health.
6. Describe the effects of reactive oxygen species in disease conditions.
Level 3
1. Explain the biomedical importance of oxidative phosphorylation.
2. Describe mitochondrial shuttles.
3. Describe the role of mitochondria in cellular energy production.
4. Describe the causes and consequences of mitochondrial disorders.
5. Describe the role of mitochondria in health and diseases.
6. Describe the biomedical importance of oxidative stress.
7. Explain the consequences of imbalance between oxidants and anti-oxidants in the body.
Energy MetabolismContent
• Sources and utilization of energy
• Energy balance and its regulation
• Metabolic rate (MR) and Basal Metabolic rate (BMR)
• Factors affecting MR and BMR
• Applications of BMR in clinical medicine
• Obesity
Objectives
Level 1
1. Define metabolism, energy and energy metabolism.
2. Describe energy balance of the body.
3. Explain the internal utilization of energy.
4. List the sources of energy.
5. List the various methods of determining energy expenditure.
6. Describe the principles of direct and indirect methods of determining energy expenditure.
7. Define metabolic rate.
8. Describe the factors that influence metabolic rate.
9. Define basal metabolic rate.
10. Describe the factors that influence basal metabolic rate (BMR).
11. State the normal values of basal metabolic rate of adult male and adult female.
12. Describe the specific dynamic action of food.
13. Describe respiratory quotient.
14. Define energy cost.
15. State the principle of determining BMR.
16. Calculate and interpret the BMR of an individual by the given data.
17. Describe the applications of BMR to clinical medicine.
Level 2
1. Describe the biochemical basis of obesity.
Carbohydrate MetabolismContent
• Overview of carbohydrate metabolism
• Fate of glucose, Fate of glucose 6-phosphate
• Glycolysis and its biomedical importance
• Fate of pyruvate and clinical aspect of pyruvate metabolism
• Hexose monophosphate shunt and its biomedical importance
• Uronic acid pathway and its significance
• Glycogen metabolism
• Gluconeogenesis and its metabolic significance
• Citric acid cycle and its metabolic significance
• Blood glucose regulation
• Metabolisms of fructose and galactose, and their metabolic significance
• Glucose tolerance test
• Glycated protein in diabetes and its significance
Importance of glycated haemoglobin (HbAlc), sorbitol pathway and oxidative stress in development of diabetic complications
Objectives
Level 1
• Define
a. Glycolysis (e) HMS pathway
b. Glycogenesis (f) Uronic acid pathway
c. Glycogenolysis (g) Citric acid cycle
d. Gluconeogenesis
• State the overview of carbohydrate metabolism.
• Outline the metabolic fates of glucose in a cell.
• Outline the Embden-Meyerhoff pathway (glycolysis) with key enzymes.
• State the regulation of glycolysis in key steps.
• Denote the energy-producing sites in Embden-Meyerhoff pathway (glycolysis).
• State the total number of ATP produced when one molecule of glucose is oxidized through glycolysis.
• Describe the fate of pyruvate.
• Outline hexose monophosphate shunt with key enzymes and state the control of key steps.
• Outline uronic acid pathway.
• Describe the metabolic significance of Embden-Meyerhoff pathway (glycolysis), hexose monophosphate shunt and uronic acid pathway.
• State the differences between hexokinase and glucokinase.
• Describe the metabolic significance of Krebs' Cycle.
• Describe the importance of NADPH in the body with examples.
• List the sites for glycogenesis and outline glycogenesis with key enzymes.
• State the allosteric and hormonal control of glycogenesis.
• Outline glycogenolytic pathway with key enzymes.
• State the allosteric and hormonal control of glycogenolysis.
• Describe the reciprocal control of glycogenesis and glycogenolysis.
• Describe the metabolic significance of glycogen metabolism.
• List gluconeogenic compounds.
• Outline gluconeogenic pathway with key steps.
• Describe the metabolic significance of gluconeogenesis.
• State the control of gluconeogenesis.
• Explain Cori cycle and glucose-alanine cycle and state their importance.
• State the differences between glycolysis and gluconeogenesis.
• State the reciprocal control of glycolysis and gluconeogenesis.
• List the sources of blood glucose during fed state and fast state.
• State the normal fasting blood glucose level (FBS) and two-hour blood glucose level (RBS) in conventional unit and SI unit.
• State the renal threshold level of glucose in conventional unit and SI unit.
• List the organs involved in blood glucose homeostasis and describe the roles of each organ.
• List hyperglycemic and hypoglycemic hormones and describe the effects of these hormones on blood glucose level.
• Describe blood glucose homeostasis in the fed (absorptive) and fast (postabsorptive) states.
• State the principles of the different methods for determination of blood glucose level.
• State the control of gluconeogenesis.
• Explain Cori cycle and glucose-alanine cycle and state their importance.
• State the differences between glycolysis and gluconeogenesis.
• State the reciprocal control of glycolysis and gluconeogenesis.
• List the sources of blood glucose during fed state and fast state.
• State the normal fasting blood glucose level (FBS) and two-hour blood glucose level (RBS) in conventional unit and SI unit.
• State the renal threshold level of glucose in conventional unit and SI unit.
• List the organs involved in blood glucose homeostasis and describe the roles of each organ.
• List hyperglycemic and hypoglycemic hormones and describe the effects of these hormones on blood glucose level.
• Describe blood glucose homeostasis in the fed (absorptive) and fast (postabsorptive) states.
• State the principles of the different methods for determination of blood glucose level.
• State the principles and interpret the levels of fasting blood glucose, random blood glucose (two-hour blood glucose level) and the glucose tolerance test (GTT).
• Perform the estimation of blood glucose by glucose oxidase method.
• Interpret the normal and low tolerance curves with the given data of GTT.
• Outline the metabolisms of fructose and galactose in the liver.
• State the metabolic significance of galactose.
• State the clinical significance of fructose.
• Describe the role of liver in carbohydrate metabolism.
Level 2
State the general concept of intermediary metabolism.
• State the metabolic significance of hexokinase and glucokinase.
• State the clinical significance of pyruvate kinase deficiency and glucose 6phosphate dehydrogenase (G6PD) deficiency.
• Correlate the defective enzymes of glycogen metabolism with glycogen storage diseases.
• State the significance of the enzyme galactose uridyltransferase.
• State the structures of the different types of glycosaminoglycans.
• State the metabolic significance of the different types of glycosaminoglycans.
• Differentiate glycosaminoglycans and proteoglycans.
• State the biochemical importance of glycosaminoglycans and glycoproteins.
Level 3
• Describe the enzyme-mediated regulation of carbohydrate metabolism.
• Correlate the biochemical changes in diabetes mellitus with diabetic complications.
• Correlate the levels of HbA1c in diabetic control.
• State the clinical significance of polyol pathway.
• Explain the mechanisms of oxidative stress in diabetes.
Lipid MetabolismContent
Overview of lipid metabolism
• Metabolism of fatty acid
• Metabolism of ketone bodies and clinical significance
• Metabolism of triacylglycerol and significance
• Metabolism of adipose tissue and significance
• Metabolism of eicosanoids and significance
• Metabolism of phospholipids and significance
• Metabolism of cholesterol: biosynthesis, regulation of biosynthesis
• Blood cholesterol level and controlling factors
• Lipid transport: metabolism of lipoproteins and significance
• Importance of lipid peroxidation
Importance of abnormal lipoprotein metabolism in obesity, atherosclerosis and fatty liver.
Objectives
Level 1
1. Outline the overview of lipid metabolism.
2. List metabolically significant plasma lipids.
3. State the normal concentrations of the metabolically important plasma lipids.
4. Define lipogenesis.
5. List the sources of fatty acids in cell.
6. Outline fatty acid synthesis including site, important materials, and key enzymes.
7. State the regulation of fatty acid synthesis.
8. List different pathways of fatty acid oxidation and significance of each.
9. Define -oxidation.
10. Describe -oxidation.
11. Calculate the energy yielding of major plasma fatty acids (palmitic acid & stearic acid) via -oxidation and complete oxidation in CAC cycle.
12. State the structure of triacylglycerol.
13. Outline triacylglycerol synthesis including sites and important materials.
14. Describe lipolytic pathway with key enzymes and conditions.
15. Describe the hormonal regulation of lipolysis.
16. Describe the factors affecting plasma free fatty acid level.
17. Define and list essential fatty acids.
18. List the major groups of eicosanoids.
19. Outline the synthesis of different types of eicosanoids from arachidonic acid.
20. Differentiate the structures of phospholipids and glycolipids.
21. State the metabolic significance of phospholipids and glycolipids.
22. List the ketone bodies and state the normal blood level.
23. Outline ketogenesis including site, enzymes, important materials and regulation.
24. Describe the utilization of ketone bodies.
25. Describe the conditions causing ketosis.
26. State the normal total blood cholesterol, HDL-cholesterol, VLDL-cholesterol, LDLcholesterol and triacylglycerol levels.
27. List the sources of blood cholesterol and the sites of cholesterol synthesis.
28. Outline the steps involved in biosynthesis of cholesterol.
29. Outline the control of cholesterol biosynthesis.
30. State cholesterol balance in the cell.
31. Describe the functions of cholesterol.
32. Describe the factors affecting the blood cholesterol level.
33. Outline cholesterol excretion from the body.
34. List lipoproteins present in blood.
35. State the formations of lipoproteins.
36. State the functions of apolipoproteins.
37. State the functions of lipoproteins.
38. List the lipoproteins involved in cholesterol transport.
39. Describe lipoprotein metabolism.
40. Describe the role of liver in lipid metabolism.
41. State the principles of the determinations of HDL-cholesterol by Lopes method, total serum cholesterol by Zlatkis method, and triacylglycerol by enzymatic colorimetric method with lipid clearing factor.
42. Calculate plasma LDL-cholesterol and VLDL-cholesterol by using Friedewald formula.
43. Interpret lipid metabolism of an individual by the given data of lipid profile.
Level 2
1. Describe adipose tissue metabolism.
2. State the clinical significance of eicosanoids in inflammation.
3. Describe the metabolism of eicosanoids.
4. Describe the metabolism of unsaturated fatty acids.
5. Define lipid peroxidation and state its effect on cell and body functions.
6. Differentiate the major metabolic significance between white and brown adipose tissues.
7. Outline the biochemical basis of fatty liver.
Level 3
1. Describe lipid metabolism during fed state and fast state.
2. Describe the biomedical importance of lipoproteins.
3. Describe the role of LDL and HDL lipoproteins in atherosclerosis.
4. Outline the ethanol metabolism in the liver and its clinical significance.
5. State the relationship between carbohydrate and lipid metabolisms through major metabolic pathways.
6. Understand the biochemical basis of metabolic syndrome.
Protein Metabolism Content
• Overview of amino acid metabolism
• Biosynthesis of nutritionally non-essential amino acids
• Protein degradation
• Catabolic fate of amino acids
• Metabolism of ammonia and its significance
• Urea cycle, blood urea and its significance
• Anabolic fate of amino acids
• Conversion of amino acids to specialized products and neurotransmitters
• Disorders of protein degradation and amino acid metabolism
• Amino acid pool
Specialized proteins of extracellular matrix: collagen, elastin, etc.
Objectives
Level 1
1. Outline the overview of amino acid metabolism.
2. State the derivation of nutritionally non-essential amino acids from intermediary compounds.
3. Describe the anabolic fate of amino acids in the body.
4. State the role of ubiquitin in protein degradation.
5. Describe the catabolic reactions of amino acids in the body.
6. Relate the role of vitamin B6 in amino acid metabolism.
7. State the fate of carbon skeletons of amino acids.
8. List the sources of blood ammonia and state the normal blood ammonia level.
9. Describe the mechanisms and importance of the removal of ammonia.
10. Describe urea cycle with diagram.
11. State the normal blood urea level in conventional unit and SI units.
12. Describe the factors affecting the blood urea level.
13. State the mechanism of ammonia toxicity.
14. State the principle of the determination of blood urea by diacetylmonoxime method.
15. Perform the estimation of blood urea level.
16. Interpret the renal function of an individual by the given blood urea level.
17. Describe amino acid pool.
18. State the normal plasma amino acid concentration.
19. State the normal plasma amino nitrogen level.
20. State the conversion of amino acids to specialized products.
21. Describe the role of liver in protein metabolism.
Level 2
1. State the clinical significance of blood ammonia.
Level 3
1. State the disorders of protein degradation.
2. State the metabolic disorders of urea cycle.
3. State the defects in the metabolic pathways of amino acids.
Nucleoprotein Metabolism Content
• Biomedical importance of nucleotides
• Synthesis of purine nucleotides
• Catabolism of nucleic acids: Outline of pathway of purine breakdown
• Blood uric acid: Factors affecting the blood urine acid level
• Metabolism of pyrimidine: outline of synthesis and breakdown
Objectives
Level 1
1. List the components of nucleoproteins
2. Describe the biochemical functions of nucleotide.
3. Name the sources of carbon and nitrogen atoms of purine and pyrimidine rings.
4. State the different synthetic pathways of purine and pyrimidine nucleotides.
5. 5. Outline the synthesis of purine and pyrimidine nucleotide synthesis
6. Describe the catabolism of purine.
7. State the normal blood uric acid level of an adult.
8. Describe the factors affecting blood uric acid level.
9. State the principle of the determination of blood uric acid by Hanari method.
10. Interpret the purine metabolism of an individual by the given uric acid level.
11. List the foods rich in nucleic acids.
12. List the end products of purine and pyrimidine catabolisms.
Level 2
1. (List the foods rich in nucleic acid.)
2. State the clinical significance of the defective enzymes: HGPRT, adenosine deaminase and xanthine oxidase.
3. State the clinical significance of gout.
Level 3
1. Explain the basic principle of the usage of base analogs in clinical medicine.
2. State the defects in metabolic pathways of purine metabolism.
Integration of Metabolism and Common Metabolic Pool Content
1. Interpret the purine metabolism of an individual by the given uric acid level.
2. List the foods rich in nucleic acids.
3. List the end products of purine and pyrimidine catabolisms.
Level 2
1. (List the foods rich in nucleic acid.)
2. State the clinical significance of the defective enzymes: HGPRT, adenosine deaminase and xanthine oxidase.
3. State the clinical significance of gout.
Level 3
1. Explain the basic principle of the usage of base analogs in clinical medicine.
2. State the defects in metabolic pathways of purine metabolism.
Integration of Metabolism and Common Metabolic Pool Content
1. Common metabolic pool
2. Role of liver in metabolism
3. Metabolic changes during fed state and fast state
4. Metabolic disorders in diabetes, atherosclerosis, obesity
Objectives
Level 1
1. Define common metabolic pool.
2. List the compounds of the common metabolic pool.
3. Describe the functions of each compound of common metabolic pool.
4. Describe the metabolic fates of glucose 6-phosphate, pyruvate and acetyl-CoA.
5. Describe the strategies of metabolism.
6. Describe the regulatory mechanisms of the metabolic pathways in the body.
7. Explain the regulatory mechanisms of metabolism by compartmentation with examples.
8. Describe the role of the metabolic junctions or cross-road molecules.
9. Describe the role of liver in carbohydrate, lipid and protein metabolisms.
Level 2
1. Describe the biochemical changes during well-fed state.
2. Describe the biochemical changes during fasting state.
3. Describe how body adapts metabolically to starvation.
Level 3
1. Describe the changes of metabolism during exercise.
2. Describe the metabolic changes in malnutrition (undernutrition or overnutrition).
Medical Ethics Objectives
Level 1
1. Describe the informed consent in research.
2. Describe the researcher-subject relationship.
3. List the safety measures in laboratory.
4. Explain the importance of ethical consideration in laboratory procedures.
5. State the researcher ethics.
Teaching Learning Method
• Lectures
• Tutorials
• Practical
• Students’ Activities
Module – 1 (Basic Medical Biochemistry and Research Methodology)
1.1. Structure and functions of Biomolecules:
Learning objectives
At the end of the course student should be able to
Contents
Introduction to Biochemistry
Major complex molecule of cells and organelles of eukaryotes
Chemical structure and function of different classes of carbohydrate found in human body; monosaccharide, disaccharides, polysaccharides, homopolysaccharide, heteropolysaccharide and glycoprotein
Amino acids
Classification according to their structure and charge
Role of amino acid in protein conformation
Protein
Classification of protein
Structural organization of protein
Protein folding and pathologic consequence from perturbation of protein conformation
Chaperone
Alzheimer's disease, Parkinson’s disease, amyloidosis, Prions disease etc.
Hemoglobin and myoglobin
Structure and function relationship of hemoglobin
Structure and function relationship of myoglobin
Hemoglobinopathies and biomedical implications; HbS, HbM, thalassemia etc.
Chemical structure and role of different lipids in the body
Fatty acids
Triacylglycerol
Complex lipids; Phospholipids and glycolipids
Lipoproteins
Cholesterol
Nucleotides
Chemical composition and structure of nucleic acids; DNA and RNA
6. Extracellular Matrix
Molecular composition and structure of extracellular matrix
Extracelluar matrix in tissue homeostasis and ageing
Objectives
At the end of the course, students should be able to
Contents
Structural and molecular basis of biologic membrane
The major lipids in mammalian membranes
Membrane proteins
The fluid mosaic model of membrane structure
Architecture of lipids and proteins in membrane
Turnover of membrane lipids and proteins
Lateral diffusion of lipids and certain proteins
Transverse movements of lipids across the membrane (Flip flop)
Dynamic nature of membrane
Isolation of specific membrane components by appropriate separation techniques
Isolation of many membranes in a cell plasma membrane, mitochondrial
membrane, nuclear membrane, lysosomal, peroxisomal, endoplasmic
reticulum, golgi apparatus and others (involving centrifugation)
Determining lipid composition (TLC, GLC and GLC-MS enzymic degradation)
Determination of protein composition (SDS-Gel electrophoresis), complete analysis
of proteins (Sequencing, X-ray crystallography, NMR spectroscopy)
Functions of membrane proteins: measure specific enzymes (eg. Na+-K+ ATP ase)
Cell biology approach: Use of fluorescent dyes
Diseases or pathologic states resulting from or attributed to abnormalities of membranes
Mutation in membrane receptors and ion channels
Receptor defect due to infection
Structural abnormalities of membrane
Red cell abnormalities
Lysosomal abnormalities
Hyaline membrane disease
2.1. Enzymology and Bioenergetics
Definition and Classification,
Basic principle of enzyme catalyzed reaction
Chemical nature of enzyme; elements of enzyme structure that explain their substrate specificity and catalytic activity
Michaelis-Menten kinetics
Factors affecting velocity of enzyme reaction
Enzyme Inhibition and kinetic analysis of different types of inhibitors
Drug targeting on enzyme-catalyzed process
Regulation of enzyme activity in body homeostasis
Regulation of catalytic efficiencies
Regulation of quantity
3. Enzyme in clinical medicine
Laboratory enzymology
Enzyme and isoenzyme in diagnosis
Liver enzymes and drug metabolism
2.2. Bioenergetics
Gibb’s free energy
Free energy change
Coupling of exergonic and endergonic reactions in cellular metabolism
3. Intermediary metabolism
1. Introduction to metabolism
Major metabolic pathways and their significance
Role of enzyme and compartmentation in regulation of metabolism.
2. Carbohydrate metabolism
Digestion & absorption of carbohydrate in human GI tract
Major pathways of glucose metabolism; Glycolysis, CAC, the Pentose Phosphate Pathway, Gluconeogenesis and Glycogen metabolism
Blood glucose homeostasis
3. Lipid metabolism
Digestion & absorption of lipids in human GI tract
Metabolisms and their regulation of major lipids
Fatty acid metabolism
TAG metabolism
Cholesterol metabolism
Ketone body metabolism
4. Lipid transport and storage
Lipoproteins
Adipose tissue and TAG storage
5. Disease associated with impaired lipid metabolism
Dyslipidemia and coronary artery disease
Lipid storage diseases
6. Protein metabolism
Digestion & absorption of protein in in human GI tract
Biosynthesis of non-essential amino acids, synthesis of specialized compounds derived from amino acids
Protein turnover
Amino acid Catabolism
Fate of amino nitrogen
Fate of carbon skeleton
Clinical importance of hyperammonemia
7. Nucleotide metabolism
Purine metabolism
Biosynthesis of purine nucleotides and its regulation
Catabolism of purine nucleotides and its clinical importance
Pyrimidine metabolism
Biosynthesis of pyrimidine nucleotides its regulation
Catabolism of pyrimidine nucleotides and its clinical importance
8. Inborn error of amino acid metabolism
4. Research Methodology and Biostatistics
Objective
At the end of this chapter students are expected to gain knowledge on:
Content
Laboratory work
1. Principles of various laboratory analytical methods
Basic principles of various laboratory analytical methods
Steps in collection of blood samples and anticoagulants
Preparation of reagents
Principles in making a solution
Molarity, percent solution
Storage of stock solution
Buffer solution
2. Basic Laboratory Procedures
2.1 Photometry (Colorimetry, spectrophotometry and enzyme linked immunosorbent assay)
Types of autoanalyzers; semi-auto analyzer, Batch analyzer, random access auto-analyzer
Steps in automated system
Operation procedures and Responsibilities in maintenance of analyzer
2.2 Separation techniques (Electrophoresis and Chromatography)
- Electrophoresis
Introduction to general principles of electrophoresis
Force acting on the component in an electrophoresis system
Factors affecting electrophoresis,
Types of electrophoresis and their applications
- cellulose acetate
- agarose gel, polyacrylamide gel electrophoresis
2.3. Chromatography
Introduction to general principle of chromatography
Classification of chromatography
Principle of Partition Chromatography & procedure
Other chromatographic techniques- Adsorption chromatography, thin layer chromatograph (TLC), Gas Liquid Chromatography (GLC), High Performance Liquid Chromatography (HPLC), Affinity Chromatography, Ion exchange Chromatography
3. Laboratory safety
Laboratory common hazards, safety rule and safety procedures
Laboratory safety levels
4. Quality assurance and quality control of the laboratory
Definition of quality assurance and quality control in the laboratory
Quality control tests in clinical laboratory
Quality Control Manual vs Automation in clinical laboratory
Calibration curve
The Levey-Jennings (L-J) chart
Internal and external quality control program- External Quality Control
program
Importance of quality control of the laboratory procedures in diagnosis and
management
5. Blood chemistry
Measures chemical in the sample of blood and its association with functions of organ and
metabolism. It is important for diagnosis and prognosis. It includes measure of enzyme
activity, lipids, glucose etc.)
6. Laboratory management; Principles and processes
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Module -2
1. Human genome organization, nucleic acids and gene expression and proteomics
Objective
At the end of this chapter students are expected to
Contents
7. Polygenic and monogenic diseases
2. Molecular oncology (1 credit)
Objective
At the end of this chapter students are expected to
Contents
1. Cell proliferation and its regulation
Meiosis, Mitosis and the normal cell cycle
Role of cyclin and cyclin dependent protein kinase in cell cycle progression
Retinoblastoma and restriction point
Cell cycle check points and its regulatory proteins
2. Oncogenes and its importance in the development of cancer
Protooncogene and oncogene
Mechanisms of oncogene products in oncogenesis
3. Apoptosis
Stimuli for apoptosis
Mechanism of apoptosis
Deviation from normal apoptotic process and diseases
3. Population Genetics and Bioinformatics
Objectives
At the end of the course, students should be able to
1. Explain the basic concepts of genetics and population genetics
2. Discuss the Darwin theory of evolution and Mendel’s law of inheritance
3. Understand the age of molecular genetics
4. Discuss the principle behind the nucleotides and protein sequence alignment, PCR
primer design and protein-protein interactions.
5. Understand the principles of phylogenetic tree and on interpretation of the results
6. Edit and analyze the sequences using relevant square such as BioEdit and MEGA.
Contents
Cell theory
Mendel’s law of heredity
Darwin’s theory of evolution
Chromosome theory of inheritance
Elucidation of DNA structure to exploration of the human genome project
4. Biochemical immunology
Objectives
At the end of the student course, students should have a good understanding of ;
Contents
1. Cells of immune system and messenger proteins
2. Three levels of defense
Physical barrier
Innate immunity
Adaptive immunity
3. Complement proteins
4. Cellular basis of antibody production
5. The structure and function of the immunoglobulins
6. Membrane receptors for antigen
7. Molecular basis and signaling of immune effector molecules
Cytokines, chemokines and their signaling mechanisms
8. Regulatory mechanisms of immune system
Stem cell therapy and transplantation, immunotherapy
Tumor immunology, immunodeficiency
Autoimmune diseases
Vaccine development
Immunodiagnostic and laboratory skills and techniques
Laboratory Works
Recombinant DNA Technology
Objective
2. Demonstrate the practical laboratory skills in DNA extraction and amplification by
polymerase chain reaction.
3. Know the basic concepts on analysis human genes and chromosomes
Content
Nucleic acid extraction by various methods
PCR and quantification
Gel electrophoresis for DNA separation and identification
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Module -3
1. Nutrition and Health
Learning objectives
At the end of the course student should be able to
Contents
1. Food and balance diet
Essential nutrients and dietary reference intake
Requirement of major nutrients at different physiological states of life cycle and ill
patients
2. Metabolism of micronutrients; vitamins and minerals
Dietary sources, absorption, transport and storage
Elimination from body
3. Micronutrients and their role in growth, metabolism, wellbeing and disease prevention
Role of vitamins and minerals in metabolism, oxidative stress, bone growth
Role of vitamins and minerals in blood functions (oxygen transport, coagulation, blood
cell maturation)
4. Malnutrition
Nutritional deficiency and related diseases
Nutrition and development of chronic diseases, such as obesity, cardiovascular
disease, cancer, diabetes, etc.
5. The biological determinants of nutritional requirements and the assessment of nutritional
status in individuals
Anthropometry
Laboratory tests
Dietary history and other relevant history
6. Nutrigenomics
The relationship between nutrition and genetics
Role of genetic variation and individual dietary response
Role of nutrients in gene expression
2. Acid base, body fluid and electrolytes (Renal, blood and respiration)
Objective
At the end of the course student should be able to
Contents
1. Importance of acid base homeostasis for normal cellular processes
2. Acid base principles and Regulation of pH
Application of Henderson Hasselbalch equation
Role of buffers, lungs and kidney in acid base regulation
3. Acid base disorders: definition, causes, compensation, correction and approach to
differential diagnosis
Metabolic acidosis
Metabolic alkalosis
Respiratory acidosis
Respiratory alkalosis
4. Assessment of electrolytes and anion gap in acidosis
5. Arterial blood gas analysis
Components of arterial blood gas analysis
Step wise interpretation of data of patient’s ABG
3. Endocrinology
Objective
At the end of the course student should be able to
Content
1. Endocrine glands, chemical structure of hormones and their properties
2. Components of signaling pathways and their biomedical importance
Receptors of signaling molecules
Role of intracellular mediators, different kinases in signaling and pharmacological
agents targeting them in treatment of a variety of diseases
3. Biosynthesis, secretion, regulation of secretion, functions of hormones and their
association with disease;
Hormones of Hypothalamo pituitary thyroid glands
Hormones of Hypothalamo pituitary adrenal glands
Hormones of Hypothalamo gonadal axis
Hormones of pancreas
Hormones of adrenal medulla
Hormones of posterior pituitary
Sex hormones
Adipokines
4. Biochemical basis of the development of endocrine disorders
Insulin resistance, diabetes mellitus
Metabolic syndrome
Thyroid disorders
Osteoporosis
Cushing’s syndrome and Addison’s disease
5. Signal transduction and oncogenesis
Deregulation of signaling pathways and oncogenesis
Association of growth factors signaling and cell cycle activation and cancer
6. Laboratory diagnosis of endocrine disorders and interpretation of data of clinical cases
7. Fluid and electrolyte disturbances in endocrine disorder and other diseases
4. Hepatobiliary and Gastrointestinal function
Objective
At the end of the course student should be able to
Contents
Markers of liver dysfunction
Markers of hepatocellular injury
Markers of cholestasis
Markers of hepatocellular carcinoma
Laboratory work
Renal function tests
Liver function tests
Hormone assays
-Determination of thyroid hormones and insulin by ELISA
Determination of commonly measured analytes of the given sample or subject
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Clinical based-training (Clinical Biochemistry Part II)
Biochemical aspects of medical problems solving in
