BIOCHEMISTRY

GOAL
The broad goal is to teach Biochemistry to undergraduate students to make them understand
the scientific basis of the life processes at the molecular level and to orient them towards the
application of the knowledge acquired in solving clinical problems.

OBJECTIVES

A. KNOWLEDGE
At the end of the course, the student should be able to:

1. Describe the molecular and functional organization of a cell and its subcellular
components;
2. Delineate structure, function and inter-relationships of biomolecules and consequences
of deviation from normal;
3. Summarize the fundamental aspects of enzymology and clinical application wherein
regulation of enzymatic activity is altered;
4. Describe digestion and assimilation of nutrients and consequences of malnutrition;
5. Integrate the various aspects of metabolism and their regulatory pathways;
6. Explain the biochemical basis of inherited disorders with their associated sequelae;
7. Describe mechanisms involved in maintenance of body fluid and pH homeostasis;
8. Outline the molecular mechanisms of gene expression and regulation, the principles of
genetic engineering and their application in medicine;
9. Summarize the molecular concepts of body defence and their application in medicine;
10. Outline the biochemical basis of environmental health hazards, biochemical basis of
cancer and carcinogenesis;
11. Familiarize with the principles of various conventional and specialized laboratory
investigations and instrumentation analysis and interpretation of a given data;
12. Suggest laboratory investigations to support theoretical concepts and clinical
diagnosis.

B. SKILLS:
At the end of the course, the student should be able to:

1. Make use of conventional techniques/instruments to perform biochemical analysis

relevant to clinical screening and diagnosis;
2. Analyze and interpret investigative data;
3. Demonstrate the skills of solving scientific and clinical problems and decision making;

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C. INTEGRATION
The knowledge acquired in Biochemistry should help the students to integrate molecular
events with structure and function of the human body in health and disease.

COURSE CONTENT AND TEACHING HOURS

A. TEACHING HOURS

Curricular component Time allotted in hours

Lectures 80
Small group teaching / tutorials / integrated learning /practical 150
Self-directed learning 20
Early clinical exposure (basic science correlation and clinical 30 (18 +12)
skills)
Total 280
AETCOM module 1.4 7

B. Course content
(i) Theory Topics

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Syllabus

Teaching hours – 160 hours

Sl Topic (Competency No) No.

1. Relevance of Biochemistry in Medicine Core: 1 hr
Importance of Biochemistry in health and disease - (Orient
Examples of normal biochemical process ation
- Examples of biochemical derangements involved in disease development lecture)
- Examples of application of laboratory medicine in screening, diagnosis and
prognosis of diseases
2 Cell and organelles, Cell membrane, Transport across cell membranes (BI1.1) 2 hrs
Core:
Prerequisite: Concept of prokaryotic and eukaryotic cell
Cell organelles – Structure, Biochemical functions, Marker enzymes
Cell Membrane - Fluid mosaic model, composition, Fluidity of membrane
Transport across cell membranes with examples
Passive transport – Diffusion and facilitated transport (ion channels)
Active transport – Primary and Secondary
Endocytosis and Exocytosis
Aquaporins
ABC family of transporters
Non core:
Cytoskeleton –
Structure and functions of microtubules, actin filaments, intermediate filaments
Intercellular communication
Separation of cell organelles 9 hrs
3 Enzymes (BI2.1, BI2.3, BI2.4, BI2.5, BI2.6, BI2.7)
Core:
Enzymes- Definition, General properties, IUBMB Classification.
Coenzymes and Cofactors
Mechanism of Enzyme action - Concept of activation energy, transition state, binding energy, active
site; Substrate binding to active site - Koshlands Induced fit theory
Factors affecting enzyme activity
Effect of substrate concentration - Michaelis -Menton theory, Km value, Vmax and its significance
(derivation not required)
Enzyme specificity
Enzyme inhibition - Competitive and Non-competitive inhibition with examples of clinical
importance
Suicide inhibition
Enzymes as toxins – Eg. Snake venom phospholipase
Enzyme regulation by- Short term (Covalent modification, Zymogen activation,

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Allosteric regulation, Feedback regulation) and long term regulation (Induction
and repression)
Clinical Enzymology – Concept of plasma functional and non-functional enzymes
Diagnostic Importance of enzymes – LDH, CK, AST, ALT, ALP, GGT, Amylase,
Lipase, G6PD, Cholinesterase, ACP, 5’nucleotidase
Isoenzymes – Definition, Diagnostic Importance of isoenzymes with examples.
Enzymes as Therapeutic agents
Enzymes used in diagnostic assays
Ribozymes
Non core:
Mechanisms of enzyme catalysis (List)
4 Chemistry of Carbohydrates (BI3.1) 3 hrs
Core:
Definition, Biomedical importance
Classification with examples
Monosaccharide derivatives – Uronic acids, aminosugars, Glycosides, Sorbitol,
Mannitol and their Clinical significance.
Disaccharides, oligosaccharides -composition, importance
Polysaccharides –Homopolysaccharides – Composition and Importance of starch,
glycogen, Dextran, Cellulose and Inulin.
Heteropolysaccharides – Mucopolysaccharides (Composition and function)
Concept of glycation and glycosylation
Importance of Glycoproteins
Non core:
Sialic acid – importance
Blood group substances
5 Carbohydrate metabolism (BI3.2, BI3.3, BI3.4,BI3.5, BI3.6, BI3.7, BI3.9) 14hrs
Core:
Digestion and absorption
Mechanism of absorption
Lactose intolerance
Glucose transporters
Insulin dependent and Insulin independent uptake of glucose by tissues
PATHWAYS – Significance, Site, reactions, key steps, energetics, regulation,
inhibitors and associated disorders of -
· Glycolysis, Rapaport Leubering cycle and its significance
· Citric acid cycle, Amphibolic role, Anaplerotic reactions
· Gluconeogenesis, Cori’s cycle
· Glycogenesis, Glycogenolysis, Glycogen storage disorders
Significance of HMP shunt pathway and uronic acid pathway
Glucose-6-Phosphate dehydrogenase deficiency

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Galactosemia, Essential Fructosuria, Hereditary fructose intolerance Regulation
of blood glucose levels in well fed condition and fasting/starvation
Non core:
Galactose and Fructose metabolism
Details of Pyruvate dehydrogenase (PDH) reaction
Essential pentosuria
6 Chemistry of lipids (BI4.1, BI11.24) 3 hrs
Core:
Definition, Modified Bloor’s classification with examples.
Biomedical importance of lipids
Fatty acids - Definition, examples and importance of Essential fatty acids, Mono
and Polyunsaturated fatty acids, n3 and n6 fatty acids, Trans-fatty acids.
Triacylglycerol – composition and importance
Phospholipids - Types, functions with clinical importance
Respiratory distress syndrome
Glycolipids – Types and importance
Cholesterol - structure and biological importance
Lipoproteins - Types and functions
Amphipathic lipids - Definition, examples and importance, Liposomes
Non core:
Fatty acids – nomenclature and different types of classification
Synthesis of lung surfactant

7. Lipid metabolism (BI4.2, BI4.3, BI4.4, BI4.6) 12 hrs

Core:
Digestion and Absorption
Steatorrhea
Biosynthesis and breakdown of triacylglycerol
PATHWAYS – Significance, Site, reactions, key steps, energetics, regulation, and
associated disorders of -
Beta oxidation
Ketogenesis, ketolysis
Cholesterol biosynthesis upto mevalonate.
Other types of Oxidation of fatty acids and associated disorders
Lipoprotein metabolism Structure, Composition, Types, Functions, metabolism of
Chylomicrons, VLDL, LDL, HDL
Formation and functions of bile acids and bile salts
Fatty liver and lipotropic factors
Hyperlipoproteinemias
Biochemical basis of use of hypolipidemic drugs
Prostaglandins – types and biomedical importance
Non core:
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Fatty acid synthase multienzyme complex
Outline of Fatty acid biosynthesis
Lipid Storage Disorders
8 Chemistry of amino acids and Proteins (BI5.1, BI5.2) 3 hrs
Core:
Prerequisite: Amino acids – Classification based on side chain properties, nutritional
requirement
Classification of Amino acids based on metabolic fate
Standard and non-standard amino acids
Biologically important peptides
Proteins – Definition, Classification based on chemical nature and solubility,
functions, nutritional value
Structural organisation of proteins (primary, secondary, super secondary
structures/ motifs, domains, tertiary and quaternary structures)
Bonds stabilizing protein structure
Structure function relationship of proteins - haemoglobin, myoglobin, collagen
and Insulin
Denaturation - definition, causes, properties of a denatured protein, significance.
Non core:
Isoelectric pH
Non-protein amino acids, Non-alpha amino acids, D-amino acids
9 Protein and amino acid metabolism (BI5.3, BI5.4, BI5.5, BI11.17) 13 hrs
Core:
Digestion and absorption and associated disorders
Amino acid pool
General reactions – Transamination, Transmethylation, Transdeamination,
Deamination - Oxidative and nonoxidative and their significance.
Biogenic amines
Sources and fate of ammonia - Trapping, Transport and Disposal of ammonia,
ammonia toxicity
Urea cycle and its disorders
Amino acid metabolism
Glycine – specialised products and their importance
Phenylalanine, Tyrosine – metabolic pathway, synthesis of catecholamines.
Pheochromocytoma
Other specialised products formed from tyrosine and their importance
Tryptophan- synthesis of serotonin and melatonin and their importance
Carcinoid syndrome
Sulphur containing amino acids – functions of cysteine, methionine synthesis of
SAM, SAH, Homocysteine
Formation of Nitric oxide and its importance

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Inborn errors of metabolism – enzyme defects, clinical features, laboratory
diagnosis and biochemical basis of management of – PKU, Tyrosinosis,
Alkaptonuria, Albinism, Homocystinuria, Maple syrup urine disease (MSUD)
Important functions/products from histidine, serine, Aspartate, Asparagine,
glutamate, glutamine, serine, branched chain amino acids
Polyamines - Examples and importance
Non core:
Techniques to separate and identify amino acids.
10 Plasma proteins (BI5.2) 3 hrs
Core:
Functions and clinical significance of plasma proteins - Albumin, α, β and γ globulins.
Acute phase reactants - Positive and Negative (clinical significance)
Biological Reference range of serum total protein, albumin, total globulin, C reactive
protein
Multiple Myeloma
Non core:
Separation and identification of plasma proteins by electrophoresis and precipitation
reactions
11 Metabolism and homeostasis (BI6.1, BI3.8, BI4.5, BI4.7, BI3.10, BI11.17) 6 hrs
Core:
Metabolic processes taking place in specific organs in the body in fed, fasting and
exercise states.
Metabolic changes during starvation
Adipose tissue – Hormones secreted from adipose tissue (adipokines – leptin,
adiponectin) their functions and role in hunger and satiety.
Diabetes mellitus – types, metabolic changes, complications.
Guidelines for diagnosis of Diabetes mellitus
Artificial sweeteners- list, use, metabolic effects(briefly) and concerns (to be
discussed with in context of their use in Diabetes Mellitus).
Lipid profile, Dyslipidemia
Atherosclerosis – definition, role of lipids in atherogenesis (LDL, Oxidised LDL, Lp(a), Small
dense LDL, HDL)
Lab tests in Myocardial infarction
Non core:
Advanced Glycation End (AGEs) products
12 Biological Oxidation (BI6.6) 3 hrs
Core:
Prerequisite: Bioenergetics – Laws of thermodynamics, Free energy, Exergonic and
endergonic reactions, Chemical Coupling Redox pair, Redox potential.
High Energy Compounds – Definition, Classification, biological significance.
Transport of reducing equivalents across mitochondria

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Electron Transport Chain – Organization, components, flow of electrons.
Oxidative Phosphorylation – Sites, mechanism (Chemiosmotic theory).
Binding change mechanism of ATP synthesis by ATP synthase.
Inhibitors of Electron Transport Chain and oxidative phosphorylation. Uncouplers
and their significance.
Brown adipose tissue metabolism.
Non core:
ATP-ADP cycle.
Structure and organization of ATP synthase complex.
Mitochondrial myopathies
13 Heme metabolism (BI6.11, BI6.12, BI5.2, BI11.17) 7 hrs
Core:
Heme –Outline of Synthesis, porphyrias
Degradation of Heme, Bilirubin metabolism – synthesis, transport, conjugation,
excretion
Jaundice – definition, types, causes, lab diagnosis
Congenital hyperbilirubinemias
Hemoglobin – Adult, fetal and embryonic types
Abnormal hemoglobins– carboxy, sulph, metHb.
Hemoglobinopathies – molecular defects, pathophysiological changes in
thalassemias and sickle cell anemia
Non core:
p50 of hemoglobins
14. Extracellular matrix (BI9.1, BI9.2) 4 hrs
Core:
Composition of ECM – Proteins (Composition and functions of Collagen, elastin,
fibrillin, fibronectin, laminin) and Proteoglycans.
Involvement of ECM components in health and disease. Eg.
Osteogenesis Imperfecta, Ehler-Danlos syndrome etc
Non core:
Bone tissue– Concept of Bone turnover, factors affecting bone turnover, Peak bone
mass, List of markers of bone formation and bone resorption.
15. Vitamins (BI6.5) 12 hrs
Core:
Prerequisite: Definition, difference between water and fat soluble vitamins
RDA, Sources, Metabolism, Biochemical functions, Deficiency manifestations,
Hypervitaminoses of Fat soluble vitamins (A,D,E,K), Water soluble vitamins -
Vitamin C, Folic acid, Vitamin B12, Thiamine, riboflavin, Niacin, Pyridoxine, Biotin,
Pantothenic acid
Antivitamins
Non core:
Vitamers
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Lipoic acid

16 Minerals (BI6.9, BI6.10) 8 hrs

Core:
Major elements and trace elements
Sources, RDA, absorption and transport, Homeostasis, Functions, Biological
reference range, disorders associated with – Calcium, phosphorus, Iron
Functions and disorders associated with - Copper, Zinc, Selenium, Fluoride,
Iodine, Magnesium, Molybdenum.
17 Chemistry of Nucleic acids (BI7.1) 2 hrs
Core:
Prerequisite: Nitrogenous bases: Purines and Pyrimidines (Major, Minor, Free Bases);
Nucleosides and Nucleotides – Structure, examples, Importance
Nucleoside derivatives: NMP, NDP, NTP cAMP, SAM, PAPS, UDP sugars etc
Synthetic Nucleotide Analogues and their application
Structure and function of DNA (B-DNA)
Structural organization of DNA to form chromatin (Primary and Secondary)
Types of RNA (hnRNA, mRNA, rRNA, tRNA, snRNA) with structure and
functions
microRNA (miRNA) and small interfering RNA (siRNA) and their applications in
medicine
Non core:
Different types of DNA
18 Nucleotide metabolism (BI6.2, BI6.3, BI6.4) 4 hrs
Core:
Prerequisite: Sources of atoms of Purine and pyrimidine ring
Salvage pathways of Purine and pyrimidine synthesis
Catabolism of Purines, Uric acid and its importance
Etiology, manifestations and biochemical basis of clinical manifestations of – Gout,
LeschNyhan syndrome,
Non core:
SCID, Oroticaciduria
Diagnostic importance of Adenosine deaminase
19 Molecular Biology (BI7.1, BI7.2, BI7.3, BI9.3) 11 hrs
Core:
Concept of Genomics, proteomics and metabolomics
DNA Metabolism
Cell cycle
DNA replication - prokaryotic and eukaryotic replication, requirements, process,
inhibitors
Telomere, Telomerase and its importance
DNA repair mechanisms
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Diseases associated with DNA repair – Eg. Xeroderma Pigmentosum
Mutations, causes, types of mutation, Consequences with examples
RNA Metabolism
Transcription process
Transcriptional units, promoter regions, RNA polymerases in prokaryotes and
eukaryotes
Differences between prokaryotic and Eukaryotic transcription
Inhibitors of transcription process
Post transcriptional modifications of all types of RNA
Protein Biosynthesis
Genetic Code and its characteristics
Requirements and activation of amino acids
Translation in Eukaryotes
Inhibitors of Translation
Post translational modifications
Regulation of Gene expression
Gene, introns, exons, cistron
Regulation of gene expression in prokaryotes with illustration of Lac Operon
Regulation of gene expression in eukaryotes – Role of enhancers, repressors, DNA
regulatory elements, gene amplification, gene rearrangement, RNA processing,
RNA editing, mRNA stability.
Non core:
Role of transcriptional activators and coregulators
Protein folding – Role of Chaperones and Heat shock proteins, Alzheimers
disease, Prion diseases
Protein targeting and sorting with associated disorders Eg, I cell disease
Protein motifs in DNA regulatory proteins
Chromatin remodeling in regulation
Epigenetics
20. Molecular biology techniques and Gene therapy (BI7.4) 4 hrs
Core:
Recombinant DNA technology, DNA cloning - process and application
PCR technique and its application
Blotting techniques
Concept, types and application of gene therapy.
DNA Polymorphism, SNP, VNTR, RFLP
DNA genomic and cDNA libraries
DNA Probes
DNA Microarrays
Overview of Human Genome Project HGP
21 Biochemistry of Cancer (BI10.1, BI10.2) 5 hrs
Core:
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Cell cycle, regulation, abnormal cell growth, programmed cell death (apoptosis)
Cell signaling (action of hormones and growth factors) – Cell surface receptors - G
protein coupled signaling, catalytic receptor signaling, steroid receptor signaling.
Mutagens and carcinogens: Definitions, examples and their actions in carcinogenesis
Protooncogenes and their activation, oncogenes, tumour suppressor genes and
their role in development of cancer
Oncogenic viruses (HPV and cervical cancer)
Growth factors and their receptors
Tumour markers and their importance in diagnosis and prognosis of cancer
Biochemical basis of cancer therapy – alkylating agents, antimetabolites,
topoisomerase inhibitors, antibiotics, hormones, receptor blockers, radiotherapy etc
Monoclonal antibodies and their application
Non core:
Hybridoma technology
Estrogen and progesterone receptors and their clinical importance in breast cancer
22 Immunology (BI10.3, BI10.4, BI10.5) 1 hr
Core:
Cellular and humoral components of immune system
Immunoglobulins – Classes, structure function relationship
Innate and adaptive immune responses, self/non-self-recognition
Role of T-helper cells in immune responses
Ig class switching
Concept of Immune tolerance and Autoimmunity
Antigens and concepts in vaccine development – types of vaccines, immunological
basis of vaccine development, recombinant DNA technology in vaccine development.
Non core: Hypersensitivity reactions
Concept of graft rejection
Phases of vaccine development.
23. Nutrition and dietetics (BI8.1, BI8.2, BI8.3, BI8.4, BI8.5, BI11.17, BI11.23, BI11.24) 7 hrs
Core:
Energy content of food items
BMR – Definition, Normal values, Factors affecting and biomedical importance
SDA – Definition and significance (Thermogenic effect of food)
Nitrogen balance
Balanced diet – definition, composition
Dietary fibers – definition, examples, importance
Glycemic index – definition, calculation, importance
Nutritional importance of Carbohydrates, Lipids, Proteins, Vitamins and minerals,
commonly used food items including fruits and vegetables.
Nutritional indices
Calculation of calorie requirement

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Dietary advice for optimal health in childhood and adults, special conditions like
diabetes mellitus , coronary artery disease, pregnancy.
Types, causes and effects of Protein energy malnutrition
Obesity – Definition, BMI, types, causes, role of GI peptides and adipokines in
obesity, associated health risks (eg., metabolic syndrome)
24 Organ function tests (BI6.13, BI6.14, BI6.15, BI11.17) 11 hrs
Core:
Functions of Liver, Kidney, Thyroid and adrenals.
Liver Function Tests: Tests based on Synthetic, Excretory, and Role of enzymes in
hepatic dysfunction
Renal Function tests – Tests to assess glomerular and tubular functions
Mechanism of action of Group I and Group II hormones
Thyroid function tests
Adrenal function tests
Non core:
Lab tests for evaluation of Infertility.
25 Acid base balance (BI6.7, BI6.8, BI11.17) 4 hrs
Core:
Prerequisite: Concept of Acids, Bases and buffers, HH Equation and its application
Regulation of pH of blood by buffers, respiratory and renal mechanisms
Anion gap and its significance
Acidosis and alkalosis (metabolic and respiratory) – causes, compensatory mechanisms
and lab findings
26 Water and electrolyte balance (BI6.7) 3 hrs
Core:
Distribution of water and electrolytes in ICF and ECF
Osmolality of ECF
Regulation of water and electrolyte balance
Disorders of electrolyte imbalance – causes and clinical features of Hyperkalemia,
Hypokalemia, Hypernatremia, Hyponatremia
Dehydration
27 Free Radicals and Antioxidants (BI7.6, BI7.7) 3 hrs
Core:
Free radicals, Reactive oxygen species (ROS), Reactive nitrogen species (RNS)
Damaging effects of ROS on biomolecules, lipid peroxidation
Anti-oxidant defence system of our body – enzymes, vitamins, metabolites as antioxidants
Role of oxidative stress in atherosclerosis, diabetes mellitus and cancer
Non core:
Fenton and Haber Weiss reactions
28 Xenobiotics and Detoxification (BI7.5) 1 hr
Core:

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Xenobiotics and disease caused. Biotransformation
Phase –I reactions
Oxidation
Hydroxylation
Cytochrome P450
Phase-II reactions
Conjugation reactions-Glucuronic acid, Glutathione, Glycine
Non core:
Other detoxification reactions reduction, hydrolysis, Acetylation, Methylation and reduction
29 Clinical chemistry (BI11.16) 2 hrs
Core:
Basic concepts of clinical chemistry laboratory
Automation - advantages
Quality control concepts (Internal and external quality control, precision, accuracy)
Specimen collection and Common Preanalytical errors
Biological reference intervals
Critical alerts
Ethics in Laboratory Medicine

Note:
1. Students are expected to familiarize by themselves the contents mentioned as prerequisite (in
italics)

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 SUGGESTED DISTRIBUTION OF THEORY TEACHING HOURS
Sl Topic Suggested TL methods (hours)
No
Lecture SGT CBL Total Integration
(80) (40) (40) (160) (20)
Shared extra
hours
1 Relevance of Biochemistry in Medicine 1 Orientation lecture
2 Cell and organelles, Cell membrane, Transport 2 - - 2 2
across cell membranes

3 Enzymes 5 2 2 9 -

4 Chemistry of Carbohydrates 3 - - 3 -

5 Carbohydrate metabolism 8 2 4 14 -

6 Chemistry of lipids 3 - - 3 -

7 Lipid metabolism 8 2 2 12 -

8 Chemistry of amino acids and Proteins 3 - - 3 -

9 Protein and amino acid metabolism 7 2 4 13 -

10 Plasma proteins 1 - 2 3 1

11 Metabolism and homeostasis 2 4 - 6 2

12 Biological Oxidation 3 - - 3 -

13 Heme metabolism 3 - 4 7 2

14 Extracellular matrix 2 2 - 4 -

15 Vitamins 2 4 6 12 -

16 Minerals 2 4 2 8 2

17 Chemistry of Nucleic acids 2 - - 2 -

18 Nucleotide metabolism 2 - 2 4 -

19 Molecular Biology 7 4 - 11 -

20 Molecular biology Techniques and Gene therapy 2 2 - 4 1

21 Biochemistry of Cancer 3 - 2 5 2

22 Immunology 1 - - 1 2

23 Nutrition and dietetics 3 2 2 7 2

24 Organ function tests 1 4 6 11 2

25 Acid base balance 2 - 2 4 1

26 Water and electrolyte balance 1 2 - 3 1

27 Free Radicals and Antioxidants 1 2 - 3 -

28 Xenobiotics and Detoxification 1 - - 1 -

29 Clinical chemistry - 2 - 2 -

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Note: The above table containing teaching hours assigned to different topics
under large and small group teaching may be used as a guide by the Institutes.

i. Assessment methods for Theory (Formative and Summative):

Written (Structured Long essay Questions/Short essay questions /short
answer questions/ clinical vignette based questions)
Viva Voce
Case based learning Sessions with lab data interpretation - 20 X2=40 hrs

Sl. Topic Suggested Cases for No. of Domain Assessment Tool

No discussion sessions (2 / Level
hrs each)

1 Diagnostic enzymology Myocardial infarction 1 K/KH Case chart

BI2.7, BI11.17 Acute pancreatitis discussion /OSPE

2 Carbohydrate Diabetes Mellitus 2 K/KH Case chart

metabolism GTT charts/GST discussion /OSPE
BI3.8, BI3.10, BI11.17 Galactosemia
Von Gierke disease
3 Lipid metabolism Dyslipidemia 1 K/KH Case chart
BI3.10, BI4.7, BI11.17 Ketoacidosis discussion /OSPE
Familial
hypercholesterolemia
4 Protein metabolism PKU 2 K/KH Case chart
Inborn errors of Alkaptonuria discussion /OSPE
metabolism Homocystinuria
BI5.5, BI11.17 MSUD
Albinism

5 Plasma proteins BI5.5, Multiple myeloma 1 K/KH Case chart

BI11.16, BI11.17 discussion /OSPE

6 Nucleotide metabolism Gout 1 K/KH Case chart

BI6.4, BI11.17 discussion /OSPE

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7 Liver Function tests and Hemolytic Jaundice 2 K/KH Case chart
Hemoglobinopathies Hepatic jaundice discussion /OSPE
BI6.2, BI6.14, BI11.17 Obstructive jaundice
Neonatal jaundice
Alcoholic cirrhosis
Non alcoholic
steatohepatitis
Sickle cell anaemia
Thalassemia
8 Renal function tests Normal renal function 2 K/KH Case chart
BI6.14, BI11.17 Renal failure discussion /OSPE
Nephrotic syndrome
Acute
glomerulonephritis
9 Thyroid function tests Hypothyroidism 1 K/KH Case chart
BI6.14, BI11.17 Hyperthyroidism discussion /OSPE

10 Vitamin deficiency Vitamin A 3 K/KH Case chart

disorders BI6.5 deficiency discussion
Rickets/Osteomala /OSPE
cia Scurvy
Beri Beri
Pellagra
Megaloblastic anemia
11 Minerals BI6.10 Iron deficiency 1 K/KH Case chart
anaemia Tetany discussion
Wilson’s /OSPE
disease Goitre
Fluorosis
12 Nutritional Kwashiorkor 1 K/KH Case chart
disorders BI8.2 Marasmus discussion
Metabolic /OSPE
syndrome

13 Cancer BI10.2 Prostate 1 K/KH Case chart

carcinoma Breast discussion
carcinoma /OSPE

14 Disturbances in acid- Metabolic acidosis 1 K/KH Case chart

base balance Metabolic alkalosis discussion
BI6.8, BI11.17 Respiratory /OSPE
acidosis
Respiratory
alkalosis

110
ii. PRACTICAL: 35X2 = 70 hours

Part 1: Qualitative Experiments – 9X2=18hrs

Part 2: Quantitative Experiments – 14X2=28hrs
Part 3: Demonstration Experiments – 12X2=24hrs

Sl. Type of Suggested Teaching learning No. of Domain/ Assessment

No Experiment method - Practical tests to be practical Level method
performed classes

Part 1: Qualitative Experiments - 9 Classes

1 Analysis of DOAP sessions – Examine 3 S/P Qualitative

Normal Physical properties, Inorganic analysis
constituents constituents (Calcium,
of urine Phosphorus and Ammonia) and
BI11.3, Organic constituents
BI11.4 (Urobilinogen, Urea,
Uric acid and Creatinine)

2 Analysis of DOAP sessions - Physical 4 S/P Qualitative

Pathological examination, chemical tests analysis
Constituents of for Glucose, Ketone Bodies,
Urine BI11.4, Blood, Proteins, Bile salts and
BI11.20 Bile Pigments Demonstration
by using Dip sticks

3 Urine screening Newborn screening tests- 1 K/KH OSPE/ Viva

tests for Inborn Interpretation of laboratory
errors of reports
metabolism
BI11.5, BI5.5

4 Calculate the Small group discussion 1 K/KH OSPE/ Viva

energy – Calculate
content of
food items
11.23

111
Part 2: Quantitative Experiments - 14 Classes
1 Estimation of DOAP sessions - Perform 2 S/P Quantitative
plasma glucose and Interpret analysis/
by Enzymatic OSPE/Case
method and chart
Glucometer as interpretation
point of care
testing BI11.21,
BI3.10
2 Estimation of DOAP sessions - Perform 2 S/P Quantitative
serum and urine and Interpret analysis/
creatinine by OSPE/Case
Jaffe’s method, chart
Creatinine interpretation
clearance
BI11.7, BI11.21
3 Estimation of DOAP sessions - Perform 2 S/P Quantitative
blood urea by and Interpret analysis/
end point OSPE/Case
method chart
BI11.21 interpretation

4 Estimation of DOAP sessions - Perform 2 S/P Quantitative

Total Protein and Interpret analysis/
and Albumin OSPE/Case
in serum by chart
Biuret and interpretation
BCG method,
A:G ratio
BI11.8, BI11.21

5 Estimation Practical - Perform and 1 S/P Quantitative

of Total Interpret analysis/
cholesterol OSPE/Case
and High chart
density interpretation
lipoprotein(
HDL)
cholesterol
BI11.9

112
6 Estimation of Practical - Perform 1 S/P Quantitative analysis/
Triacylglycerols and Interpret OSPE/Case chart
BI11.10 interpretation

7 Estimation of Calcium Practical - Perform 1 S/P Quantitative analysis/

and Phosphorous and Interpret OSPE/Case chart
BI11.11 interpretation

8 Estimation of Serum Practical - Perform 1 S/P Quantitative analysis/

Bilirubin and Interpret OSPE/Case chart
BI11.12 interpretation

9 Estimation of AST, ALT Practical - Perform 1 S/P Quantitative analysis/

activity and Interpret OSPE/Case chart
BI11.13 interpretation

10 Estimation of ALP Practical - Perform 1 S/P Quantitative analysis/

activity and Interpret OSPE/Case chart
BI11.14 interpretation

Part 3: Demonstrations -12 Classes

1 Lab safety and Small group 1 K/KH Viva
Biomedical waste discussion, lab visit
disposal, Commonly
used lab equipment,
glassware and reagents
BI11.1
2 Preparation of buffers Demonstration - 1 K/KH Viva
and estimation of pH Observe
using pH meter BI11.2,
11.16, 11.19
3 Colorimetry, Demonstration - 1 K/KH Viva
Spectrophotometry Observe
BI11.6, BI11.18,
4 Clinical chemistry Demonstration - 1 K/KH OSPE/ Viva
autoanalyser and quality Observe and
control (Internal and interpret
External quality control,
Precision, Accuracy, QC
rules), Biological reference
intervals BI11.16, BI11.19

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5 Specimen collection and Collection centre 1 K/KH Viva
preanalytical errors in and lab visit
clinical Biochemistry lab

6 Serum protein Demonstration - 1 K/KH OSPE/ Viva

electrophoresis, types Observe and
and applications interpret
BI11.16, BI11.19
7 Paper Demonstration - 1 K/KH OSPE/ Viva
chromatography/TLC of Observe and
amino acids/sugars, types Interpret
and applications BI11.5,
BI5.5, BI11.16, BI11.19

8 Analysis of CSF Small group 1 K/KH OSPE/ Viva

BI11.15 discussion - Interpret
9 Estimation of serum Demonstration - 1 K/KH OSPE/ Viva
electrolytes by ISE Observe and
BI11.16, BI11.19 Interpret
10 Blood gas analysis using Demonstration- 1 K/KH OSPE/ Viva
ABG analyser Observe and
BI11.16, BI11.19 Interpret

11 Principle, procedure and Demonstration- 1 K/KH Viva

applications of ELISA, Observe
protein extraction,
Blotting techniques,
PAGE
BI11.16, BI11.19
12 Principle, procedure and Demonstration- 1 K/KH Viva
applications of PCR, DNA Observe
isolation
BI11.16, BI11.19

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 CERTIFICATION OF SKILL ACQUISITION:

To be certified using checklists

Suggested Checklist format for Certification of Skills (refer logbook)

Sl Competency to be certified with Competency number No.

No required to
1 Perform urine analysis to estimate and determine normal constituents (BI11.4) 1
2 Perform urine analysis to estimate and determine abnormal constituents (BI11.4) 1

3 Identify abnormal constituents in urine, interpret the findings and correlate 1

these with pathological states (BI11.20)
4 Demonstrate estimation of glucose in serum (BI11.21) 1
5 Demonstrate the estimation of serum Creatinine and Creatinine clearance 1
(BI11.7, BI11.21)
6 Demonstrate estimation of urea in serum (BI11.21) 1
7 Demonstrate estimation of serum protein, albumin and A:G ratio (BI11.7, 1
BI11.21)

Note: In Theory, Practicals and Certification of Skill sections, topics with corresponding
competency numbers as mentioned in Volume 1 of Competency based Undergraduate
Curriculum for Indian Medical graduate (2018), prescribed by Medical Council of India ,
have been mentioned.

iii. SUGGESTED AREAS FOR INTEGRATION:

As per the “Competency based Undergraduate Curriculum for the Indian Medical Graduate
2018: Medical Council of India”

iv. EARLY CLINCAL EXPOSURE (ECE): Needs to be entered in Log book

CLINICAL SKILLS - 12 hours Suggested cases for hospital visit
· Anemia
· Jaundice
· Renal failure
· Diabetes Mellitus
BASIC SCIENCE CORRELATION - 18 hours Suggested topics -
· Biochemical basis of myocardial infarction (dyslipidemia, atherosclerosis, diagnostic
tests)
· Biochemical basis of acute complications of diabetes mellitus
· Biochemical alterations in diarrhea (acid base and electrolyte and ORS management
· Biochemical basis of Metabolic syndrome
· Critical alerts in Biochemistry lab test results.
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 · Evidence based laboratory medicine
v. SELF DIRECTED LEARNING (SDL):
Suggested topics for log book entry in the form of concept mapping
· RBC membrane composition and Biochemical basis of Hereditary spherocytosis
· Respiratory distress syndrome
· Advanced glycation end products and complications of Diabetes
Mellitus
· Hormonal basis of osteoporosis
· Cardiovascular risk assessment score
· Biochemical basis of Alzheimer disease

AETCOM MODULES TO BE COVERED UNDER BIOCHEMISTRY:

AETCOM module number Topic
(as per MCI document)
1.4 The foundations of communication - 1

Suggested format for reflective writing for the above AETCOM modules is given in
ANNEXURE III. This could be a part of the practical record book.

SCHEME OF EXAMINATION

INTERNAL ASSESSMENT
[Kindly refer section II for general guidelines]

Scheme for calculation of Internal assessment marks:

Theory (maximum marks) Marks Practicals Marks
Theory written paper 30* Practical exam (25 marks) and viva- 30**
voce (5 marks)
Formative assessment Formative assessment

MCQs/unit 10 Early clinical exposure + Skill 5

test/seminars/assignments/ Case certification
based learning tests
Practical record 5
Total 40 40

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Please note:

*Prior to submission to the University, the marks for each of the three internal examination
theory assessments must be calculated out of 30 marks, regardless of the maximum marks.

**Prior to submission to the University, the marks for each of the three internal examination
practical assessments must be calculated out of 30 marks, regardless of the maximum marks.

Only the final marks out of 40 needs to be submitted to the University, separately for theory
and practical for each internal assessment.

UNIVERSITY EXAMINATIONS
[Kindly refer section II for general guidelines]

TABLE SHOWING SCHEME FOR CALCULATION OF UNIVERSITY EXAMINATION MARKS

Theory (maximum marks) Practical (maximum marks)

Paper 1 100 Practical exam 80
(Practical Exercise 1 to 4)

Paper 2 100 Viva-voce 20

TOTAL 200 TOTAL 100

A. THEORY: 200 Marks

There shall be two theory papers of 100 marks each and duration of each paper shall be 3
hours. The pattern of questions in each paper shall be as mentioned below

Type of Question Number of Maximum Marks Total

Questions for each question
Structured Long essay questions (SLEQ) 2 10 20
[Includes one case vignette-based question (CVBQ)]
Short ESSAY questions (SEQ) 10 05 50
[includes two case vignette-based questions
(CVBQ)]

Short answer questions (SAQ) 10 03 30

Total marks 100

Note:
1. A suggested format for blueprint of question paper is shown in Annexure I
2. Please refer Annexure II for suggested model question paper
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B. PRACTICAL:
Practical exercises – 80 marks
1. Exercise 1: OSPE - 20 Marks
2. Exercise 2: Qualitative analysis of Normal or Pathological constituents of
Urine - 20 Marks
3. Exercise 3: Quantitative estimation and interpretation - 20 Marks
4. Exercise 4: Case studies - 20 Marks

Exercise 1: OSPE (20 Marks)

No. of Stations: 4 (1 performance station, 3 response stations)
Marks for Each Station: 5
Time for each station: Max 5 min

Exercise 2: Qualitative analysis of Normal or Pathological constituents of Urine (20 Marks)

Selection, principle and performance of tests :10 marks
Interpretation and Discussion :10 marks
Note: Alphabetically arranged test procedures shall be given.

Exercise 3: Quantitative estimation and interpretation (20 Marks)

Principle:5 Marks
Performance, Calculation and Results: 5 Marks
Interpretation and Discussion:10 Marks

Note : Procedure sheets shall be given.

Exercise 4: Case studies (20marks)

Total No. of case reports: 2
1 Major Case study for 12 marks and 1 Minor Case study for 8 marks
Suggested Major Case studies: Organ function tests/Diabetes mellitus/Acid base
disorders/Myocardial infarction/ Dyslipidemia/PEM
Note : Questions for Quantitative experiments may preferably be case based scenarios.

C. Viva voce : 20 marks

The viva-voce examination shall carry 20 marks and all examiners will conduct the
examination. Viva should focus on application and interpretation. (viva marks to be
added to practical and not theory)

118
Distribution of topics for Paper 1 and Paper 2 for University examination Topic wise weightage

Sl No Paper 1 Topics Weightage Up to (in marks)

1 Cell, cellular organelles and membrane transport 5

2 Extra cellular matrix 3
3 Enzymes 13
4 Carbohydrate Chemistry 5
5 Carbohydrate Metabolism 13
6 Lipid Chemistry 5
7 Lipid Metabolism 13
8 Metabolism and homeostasis 8
9 Biological Oxidation 5
10 Vitamins 13
11 Minerals 13
12 Nutrition 10
13 Acid Base Balance 13
14 Water and Electrolyte Balance 6

Sl No Paper 2 Topics Weightage Upto (in marks)

1 Protein Chemistry 6
2 Plasma proteins 5
3 Immunology 5
4 Protein and amino acid Metabolism 13
5 Nucleic acid Chemistry 6
6 Nucleotide metabolism 10
7 Molecular Biology 13
8 Molecular Biology Techniques 13
9 Biochemistry of Cancer 10
10 Heme Metabolism 13
11 Organ function tests 13
12 Free radicals and Antioxidants 6
13 Xenobiotics and Detoxification 3
14 Clinical Chemistry 5

119
Note:
· Weightage of marks assigned to topics may add to more than 100
· Structured Long essay question should be from the topics with weightage of MORE
THAN 10 marks. However, a part of structured long essay may be from other topics
adhering to the weightage of marks allotted for that topic.
· The topics to different paper are generally evaluated under those sections. However, a
strict division of the subject may not be possible and some overlapping of topics is
inevitable. Students should be prepared to answer overlapping topics.

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 ANNEXURE I

BLUE PRINT FOR QUESTION PAPER

(to be filled by the question paper setter)

· Total marks under each type of question from each topic needs to be entered by QP Setter.
· It should be in accordance with RGUHS guideline
·
BIOCHEMISTRY PAPER 1
A B C D E G H I

Sl Topic Total SLEQ SEQ SAQ Total Higher order

No max as 10 marks 5 marks 3 marks thinking skills
per (including each marks from each questions
RGUHS one (including each topic (including
guideline CVBQ of two (total of CVBQs)
10 marks) CVBQ of columns Question Marks
5 marks) from D to number
G)
1 Cell, cellular 5
organelles and
membrane transport
2 Extra cellular matrix 3
3 Enzymes 13
4 Carbohydrate 5
Chemistry
5 Carbohydrate 13
Metabolism
6 Lipid Chemistry 5
7 Lipid Metabolism 13
8 Metabolism and 8
homeostasis
9 Biological Oxidation 5
10 Vitamins 13
11 Minerals 13
12 Nutrition 10
13 Acid Base Balance 13
14 Water and 6
Electrolyte Balance
SLEQ- Structured Long Essay Question; SEQ- Short Essay Question; SAQ- Short Answer Question ;
CVBQ- Case Vignette Based Question
Marks allocated to questions that assess higher order thinking skills (%) =

121
 BIOCHEMISTRY PAPER 2

A B C D E G H I

Sl Topic Total SLEQ SEQ SAQ Total Higher order

No max as 10 marks 5 marks 3 marks thinking skills
per (including each marks from each questions
RGUHS one (including each topic (including
guideline CVBQ of two (total of CVBQs)
10 marks) CVBQ of columns Question Marks
5 marks) from D to number
G)
1 Protein Chemistry 6
2 Plasma proteins 5
3 Immunology 5
4 Protein and amino 13
acid Metabolism
5 Nucleic acid 6
Chemistry
6 Nucleotide 10
Metabolism
7 Molecular Biology 13
8 Molecular Biology 13
Techniques
9 Biochemistry of 10
Cancer
10 Heme Metabolism 13
11 Organ function 13
tests
12 Free radicals and 6
Antioxidants
13 Xenobiotics and 3
Detoxification
14 Clinical Chemistry 5
SLEQ- Structured Long Essay Question; SEQ- Short Essay Question; SAQ- Short Answer
Question; CVBQ- Case Vignette Based Question
Marks allocated to questions that assess higher order thinking skills (%) =

Note:
1. Question paper may be framed using “Blue print “table as guideline
2. A minimum of 35% marks in each paper shall be allocated to questions that assess the
higher order thinking skills of the student. This includes Case Vignette based questions.
3. Column ‘I’ has been provided for calculating percentage of marks allotted for questions
assessing higher order thinking skills.

122
 ANNEXURE II

Rajiv Gandhi University of Health Sciences, Karnataka

First Phase MBBS Degree examination
Model Question paper
Biochemistry (RS-4)
Draw a neat labelled diagram wherever necessary

Time= Three hours Paper I Maximum marks= 100

Long essays 2X10= 20 marks

1. A 30-year-old male came to the Physician with complaints of excessive hunger, weight loss
and increased thirst since few months. Following results were obtained on testing-
i. Blood: Random Blood Sugar- 400 mg/dL
ii. Urine: Benedict’s Test – Orange precipitate
a. What is the probable diagnosis?
b. What is the biochemical basis of symptoms?
c. Name the lab tests used to monitor the patient after confirmation of diagnosis?
d. Discuss the mechanism of regulation of blood glucose levels?
(1+3+1+5=10 marks)
2. Discuss iron with respect to the following aspects-
a. Dietary sources
b. Absorption and transport
c. Deficiency manifestations
d. Laboratory findings in deficiency (1+5+2+2=10 marks)
Short essays (10X5= 50 marks)

3. A 50-year-old male presented to emergency medicine department with complaints of severe

chest pain and sweating since 6 hours. After further examination and testing, he was
diagnosed as having Myocardial infarction.
a. What would be the best marker for diagnosing Myocardial infarction in this patient
(1 mark)
b. What is the biochemical basis of using such a marker (3 marks)
c. List other markers that have been used to diagnose myocardial infarction (1 mark)
4. A 60-year-old female presented with tingling and numbness in fingers, and muscle cramps
in hands. On examination, Chvostek’s and Trousseau’s signs were observed. She had
previously undergone Thyroidectomy for Grave’s disease. Following results were obtained
on testing-
i. Serum Calcium- 6 mg/dL
ii. Serum Phosphrous – 7 mg/dL

a. What is your diagnosis? (1 mark)

123
 b. What is the biochemical basis for symptoms and laboratory findings? (3 marks)
c. Name another mineral deficiency which has similar manifestations as the above
(1 mark)
5. Discuss the metabolic changes in starvation.
6. Describe the mechanism of Oxidative phosphorylation
7. What are mucopolysaccharides. Mention the composition and biological importance of any
4 mucopolysaccharides. (1+4 marks)
8. Discuss the functions and clinical significance of lysosomes
9. Prescribe a balanced diet for a 70 kg male with moderate physical activity
10. Discuss the β-oxidation of fatty acids under following headings-
a. Biological significance (0.5 marks)
b. Steps (4 marks)
c. Energy released by oxidation of one molecule of palmitic acid (0.5 marks)
11. Give biochemical reasons for the following
a. Neurological and dermatological manifestations in Vitamin B6 deficiency (2 marks)
b. A patient on Anti-tuberculous treatment may develop Vitamin B6 deficiency (1 mark)
c. Neurological manifestations in Vitamin B12 deficiency (2 marks)
12. Explain the biochemical basis for the following-
a. LDL is called the ‘bad’ cholesterol and HDL is called the “good’ cholesterol (2 marks)
b. Fasting hypoglycemia and hyperuricemia in Von Gierke disease (2 marks)
c. Lung surfactant prevents Respiratory distress syndrome (1 mark)
Short answers (10X3= 30 marks)

13. Explain the renal regulation of pH with diagram.

14. Mechanism of Renin angiotensin system in maintaining fluid balance
15. Discuss briefly Vitamin B1 with respect to deficiency manifestations and laboratory findings
in deficiency (2+1 marks)
16. a. List two functions of collagen. (1 mark)
b. Mention the nature of collagen abnormality in (2 marks)
i. Osteogenesis Imperfecta
ii. Ehlers- Danlos Syndrome
17. Briefly explain Kohsland’s induce fit theory
18. Name essential fatty acids. Mention their biological significance (1+2 marks).
19. Differentiate between high and normal anion gap metabolic acidosis with an example.
20. Give biochemical reasons for the following-
a. Selenium has a sparing action on Vitamin E (1 mark)
b. Fluoride is used as preservative for blood glucose (2 marks)
21. Explain the metabolic changes leading to production of ketone bodies.
22. Give biochemical reasons for the following
a. Urine is acidic in metabolic alkalosis (1 mark)
b. Hyperkalemia is generally associated with metabolic acidosis (1 mark)
c. Hyperkalemia is a critical alert in laboratory (1 mark)

124
1. A guide to preparation of Case based question for Practical Examination
Q. An elderly man was brought to the emergency ward with chief complaints of nausea,
vomiting, decreased urine output, bilateral swelling of feet and increased thirst. On examination
he was lethargic, and disoriented with pedal oedema, tachycardia, BP – 100/60 mmHg, dry
tongue and decreased skin turgor.

· Interpret the history and mention the possible diagnosis.

· Write the principle and estimate the concentration of given quantitative parameter in the
sample provided and write your interpretation.
· What other biochemical investigations can be carried out to arrive at a final diagnosis?

125
 ANNEXURE III
(Note: questions could be added/modified to this document which is at the discretion of individual
institution. This appendix could be a part of practical record/logbook of Biochemistry)

SUGGESTED FORMAT FOR AETCOM SESSIONS

Name of the Facilitator: Date:

AETCOM module Number: Session number:

AETCOM Topic:

Competencies / Objectives:

1.

2.

3.

1. Briefly describe what you learnt from this AETCOM session in relation to the objectives.
(in 100-150 words)

2. Apart from the above learning, what did you observe that influenced (Positive/negative)
you during this session? (in 100-150 words)

Remarks by Facilitator:

Signature of Facilitator:
126
5. RECOMMENDED BOOKS

TEXT BOOKS: (Recent editions)

1. DM Vasudevan. Textbook of Biochemistry for Medical students
2. Lippincotts’ Illustrated reviews – Biochemistry
3. S.K.Gupta. Biochemistry for MBBS
4. Pankaja Naik. Biochemistry
5. Dinesh Puri. Textbook of Medical Biochemistry
6. Namrata Chhabra. Case oriented approach towards Biochemistry
7. Divya shanti D’sza, Sowbhagyalakhsmi. An easy guide to Practical Biochemistry.

REFERENCE BOOKS: (Recent editions)

1. Harpers’ Illustrated Biochemistry
2. Marshall and Bangert. Clinical Chemistry
3. Baynes and Dominiczak. Medical Biochemistry
4. Bhagavan and Ha. Essentials of Medical Biochemistry with clinical cases
5. Stryer. Biochemistry
6. James Watson. Molecular biology of gene

127