BCMB 200 PRACTICAL BIOCHEMISTRY I 2 Credits
Acid-Base Reactions: Titration; pH measurement; buffer preparation; determination of pK.
Acid-base reactions; buffers; chromatography; qualitative analysis of carbohydrates, proteins and lipids.
Quantitative analysis of proteins: methods for protein estimation (Folin-Lowry, Biuret, Ultraviolet absorption); determination of amino acids (ninhydrin method); preparation, purification and standardization of proteins (serum proteins, cytochrome C).
Separation Methods: Paper and gel electrophoresis; chromatography (Paper, TLC, column).
Quantitative analysis of carbohydrates: Estimation of glucose (Folin-Wu); isolation of glycogen, determination of rate of hydrolysis and chromatography of hydrolysis products.
Quantitative analysis of lipids: Solubility; emulsification; determination of iodine number and acid value; separation of serum lipids.
BCMB 201 STRUCTURE AND FUNCTION OF BIOMOLECULES 3 Credits
Chemistry & Function of Biological Compounds: Biomolecules: - monomers; polymers; macromolecules; supramolecules. Carbohydrates: - mono-, di-, oligo- and polysaccharides (structural and storage); stereoisomerism; mutarotation; reactions of carbohydrates. Other derivatives of monosaccharides. Lipids: - classification (fatty acids, triacylglycerols, phospholipids, sphingolipids, steroids, cholesterol, eicosanoids); simple lipoproteins; glycolipids (cell-cell recognition, receptors etc). Proteins: - amino acids:- basic structure, classification, acid/base properties, essential & non-essential; peptides; protein structure- primary, secondary, tertiary and quaternary structures, classification and properties. Enzymes as proteins. Nucleic Acids: - nitrogenous bases, nucleosides, nucleotides, cyclic nucleotides and nucleic acids DNA and RNAs (brief review of replication, transcription, translation). Other cellular molecules: Porphyrins, Vitamins and co-enzymes alkaloids & inorganic ions.
BCMB 202 CELL BIOLOGY I 2 Credits
Cellular Compartments of Prokaryotes and Eukaryotes: Organization, Dynamics, and Functions;
Cellular membrane systems (structure and transport); Nucleus (envelope and matrix), Mitochondria and chloroplasts (including biogenesis and evolution).
Cell Division, Differentiation, and Development: Bacterial division, Meiosis and gametogenesis; Eukaryotic cell cycles; mitosis, and cytokinesis; Fertilization and early embryonic development (including positional information, homeotic genes, tissue-specific expression, nuclear and cytoplasmic interactions, growth factors and induction, environment, and polarity); Differentiation of special cells in tissues of plants and animals.
BCMB 203 PRINCIPLES OF BIOCHEMICAL TECHNIQUES 2 Credits
Chromatography: Partition coefficient and chromatographic systems.
Basis of separation: adsorption and partition (polarity); ion-exchange (ionic nature),
exclusion/gel (molecular size and shape). Principles and applications (HPLC, FPLC,
GLC, TLC, Paper, Chromatofocusing and two-dimensional electrophoresis). Analytical
aspects: retention time and volume, capacity ratio, peak resolution theoretical plates/plate
height, peak capacity, internal and external standardization and analyte quantitation.
Centrifugation: Basic principles of sedimentation, RCF value, relationship between v, s and G. Centrifuges and rotors (types and uses). Preparative centrifugation: differential and density gradient; preparation of gradients, recovery and monitoring of fractionates. Analytical centrifugation: determination of relative molar mass (sedimentation velocity and equilibrium methods), purity and shape of macromolecules.
Electrophoresis: General principles. Low voltage thin sheets (paper, cellulose acetate, thin layer) and high voltage gels (agarose, polyacrylamide - native, gradient and SDS-PAGE). Applications; purity and molecular weight determination of proteins and nucleic acids, DNA sequencing. Iso-electric focusing and isotachophoresis.
BCMB 204 ENZYMOLOGY 2 Credits
Introduction to Enzymes: Comparison of chemical and enzyme catalysis, Activation energy and transition state, Free energy change, Chemical equilibria, Active site, Substrate specificity, Enzyme classification, enzyme assays, linked or coupled.
Factors affecting Enzyme Activity: Reaction rate (v), Effect of [S], [E], T, pH on enzyme activity; coenzyme, prosthetic groups.
Enzyme Kinetics and Inhibition: Michaelis - Menten model, Graphical representation of data (e.g. Lineweaver - Burk and Hanes plots)
Enzyme inhibition: Reversible (Competitive, noncompetitive, uncompetitive) and irreversible
Control of Enzyme Activity: Feedback regulation, allosteric enzymes, isozymes, covalent modification, activation, regulation of synthesis and breakdown (eg. lac operon, tryptophan biosynthesis).
Enzyme Purification: Cell disruption techniques, general purification strategy, enzyme assays, units of enzyme activity.
Application of enzymes in health, agriculture and industry
BCMB 205 GENERAL BIOCHEISTRY 3 Credits
Cell Structure and Function and Methods and Techniques of studying the Cell: General features of prokaryotes & eukaryotes; compartmentalization of cellular processes; Source tissue/cells selection; cell disruption and fractionation. Structure, Function and Metabolism of Carbohydrates: - mono-, di-, oligo- and polysaccharides; functions of carbohydrates; stereoisomerism; Glycolysis, substrate level phosphorylation, hexose monophosphate shunt, gluconeogenesis, synthesis of other carbohydrates from monomers, fate of pyruvate in different organisms; the electron transport chain in mitochondria and ATP synthesis. Structure, Function and Metabolism of Lipids: Different types and functions of lipids (fatty acids, triacylglycerols, phospholipids, etc); beta oxidation of fatty acids; fate of acetyl CoA units (TCA cycle, ketone bodies, cholesterol); synthesis of fatty acids. Structure, Function and Metabolism of Proteins: Amino acids: buffer solutions & buffer capacity; the Henderson-Hasselbach equation in the preparation of buffers in biological assays and systems. pKa and pI. Oxidative deamination; decarboxylation; transamination ; urea cycle; NH3 assimilation; fate of carbon skeleton (glucogenic and ketogenic amino acids); metabolism of some individual amino acids. Integration of metabolism. Protein structure, classification and functions. Enzymes: Properties & classification; factors affecting activity (co-factors & co-enzymes, pH, temp., [S], [E]); control of activity; kinetics; Michaelis-Menten equation. Nucleic acids and Protein Biosynthesis: Nitrogenous bases, nucleosides, nucleotides and nucleic acids. General overview of DNA replication, transcription and translation; Molecular basis of mutations.
BCMB 206 SPECTROSCOPIC AND RADIOISOTOPICTECHNIQUES 1 Credit
Molecular spectroscopy; molecular fluorescence; infra-red, atomic, electron spin resonance and nuclear magnetic resonance spectroscopy, mass spectrometry, X-ray diffraction and radioisotopic techniques in biochemistry, radio/fluorescent labeling (RIA, scintillation counting), autoradiography ELISA.
BCMB 207 VETERINARY BIOCHEMISTRY I 2 Credits
Cell and Tissue: Their principal chemical constituents and main metabolic activities. The characteristics of, and differences between eukaryotes, prokaryotes and viruses. Compartmentalisation and control of cellular environment. Functional role of the main cellular components; nucleus, ribosomes, Golgi bodies, endoplasmic reticulum, mitochondria and lysosomes. Biochemical technique for investigatin cell structure and function. Chemistry & Function of Biological Compounds: Biomolecules: - monomers; polymers; macromolecules; supramolecules. Carbohydrates: - mono-, di-, oligo- and polysaccharides (structural and storage); stereoisomerism; mutarotation; reactions of carbohydrates. Other derivatives of monosaccharides. Glycol-congugates: carbohydrates, sorting of molecules into-subcellular compartments, diseases of sorting. Lipids: - classification (fatty acids, triacylglycerols, phospholipids, sphingolipids, steroids, cholesterol, eicosanoids); simple lipoproteins; glycolipids (cell-cell recognition, receptors etc). Proteins: - amino acids:- basic structure, classification, acid/base properties, essential & non-essential; peptides; protein structure- primary, secondary, tertiary and quaternary structures, classification and properties. Enzymes as proteins. Nucleic Acids: - nitrogenous bases, nucleosides, nucleotides, cyclic nucleotides and nucleic acids DNA and RNAs (brief review of replication, transcription, and translation). Other cellular molecules: Porphyrins, Vitamins and co-enzymes alkaloids & inorganic ions.
BCMB 208 VETERINARY BIOCHEMISTRY II 3 Credits
Carbohydrates Metabolism: Digestion of carbohydrates, glycolysis and fate of pyruvate in different organisms; tricarboxylic acid (TCA) cycle; pentose phosphate pathway and fate of reduced coenzymes; catabolism of monosaccharides other than glucose; gluconeogenesis, Calvin Benson cycle, Cori cycle, glyoxylate cycle; glycogenesis and glycogenolysis; regulation of carbohydrate metabolism; Diseases of carbohydrate metabolism. Aerobic metabolism of pyruvate, starvation and obesity. The coenzyme role of B vitamins. Changes in nutritional requirement and metabolic rate in injury and disease. Lipids Metabolism: Digestion of triacylglycerols; the different lipases (lipoprotein lipase, hormone-sensitive lipase); fate of glycerol; beta-oxidation of fatty acids; fate of products (acetyl and propionyl CoA, ketone bodies, reduced coenzymes); synthesis of fatty acids triacylglycerol, cholesterol; regulation of metabolism. Protein Metabolism: Digestion of proteins, transamination, deamination and decarboxylation of amino acids and the fate of ammonia (urea cycle) and carbon skeleton; metabolism of specific amino acids (aromatic and sulphur-containing amino acids); synthesis of amino acids; in-born errors of amino acid metabolism; regulation of metabolism. Enzymes as biological catalyst: Enzyme kinetics and concept of rate-determining step. Enzyme specificity and allosteric regulation. Mechanisms of enzyme action and examples. Coenzymes and vitamins. Drugs and their effect on enzymes.
BCMB 212 VETERINARY BIOCHEMISTRY III 3 Credits
Glycosylation of proteins. Fibrous structural proteins. Structure and biosynthesis of collagen and elastin, intra-cellular and extra-cellular medication of proteins after translation. The collagen gene; disturbances in collagen synthesis. Diversity of protein function related to their structure. The relationship between structure and function as exemplified by haemoglobin, myoglobin and collagen. Plasma proteins. Detail of immunoglobin structure. Classes of immnunoglobin and their functions. Protein in normal disease situations. Defects in protein structure as basis of disease e. g. sickle cell anaemia. Lipid and protein components: Glycoprotein and the cell surface. Erythrocyte membrane as a model system. Blood cells: Haemopoiesi, sites of production, growth inducers, differentiation inducers. Red blood cells (erythrocytes) functions, morphology and membrane function formation and destruction, haemoglobin. White blood cells (leucocytes) types and morphology, functions, platelet functions. Blood clotting: haemostasis blood coagulation, definitions and components, mechanism of blood coagulation, anti-clotting mechanisms, fibrinolysis and haemostasis. Energetics: Chemical energy and concepts of energy transfer within cells; “high energy” compounds as “high energy currency”. Principles of energy abstraction. Energy source and utilization. Free energy and biochemical reactions (spontaneity, anabolic and catabolic reactions); metabolic reactions and ATP; energy of hydrolysis of ATP, ADP and phosphorylation products; ATP production (substrate level and oxidative phosphorylation, photophosphorylation, C3, C4); coupling reactions; uncoupling agents. Specific enzymes associated with inner and outer mitochondrial membranes, matrix and intermembrane space.Revrese electron transport, the concept of “high energy pool”. Michell’s chemiosmotic theory. Mitochondrial transport and inhibitors of mitochondrial function. Interplay of tissues, pathways and hormones in energy metabolism: Key regulatory enzymes: allosteric control of pyruvate carboxylase, phosphofructokinase, fructose 1,6-phosphate, pyruvate dehydrogenase. Effect of ATP, AMP, NADH, citrate, relevance of energy status to control. “Futile” cycles and function in thermogenesis and control sensitivity. Covalent modification: beta-adrenergic receptor and cascade processes.
BCMB 301 INTERMEDIARY METABOLISM 3 Credits
Carbohydrates: Digestion of carbohydrates, glycolysis and fate of pyruvate in different organisms; tricarboxylic acid (TCA) cycle; pentose phosphate pathway and fate of reduced coenzymes; catabolism of monosaccharides other than glucose; gluconeogenesis, Calvin Benson cycle, Cori cycle, glyoxylate cycle; glycogenesis and glycogenolysis; regulation of carbohydrate metabolism; Diseases of carbohydrate metabolism.
Lipids: Digestion of triacylglycerols; the different lipases (lipoprotein lipase, hormone-sensitive lipase); fate of glycerol; beta-oxidation of fatty acids; fate of products (acetyl and propionyl CoA, ketone bodies, reduced coenzymes); synthesis of fatty acids triacylglycerol, cholesterol; regulation of metabolism.
Amino acids: Digestion of proteins, transamination, deamination and decarboxylation of amino acids and the fate of ammonia (urea cycle) and carbon skeleton; metabolism of specific amino acids (aromatic and sulphur-containing amino acids); synthesis of amino acids; in-born errors of amino acid metabolism; regulation of metabolism.
Energetics: Free energy and biochemical reactions (spontaneity, anabolic and catabolic reactions); metabolic reactions and ATP; energy of hydrolysis of ATP, ADP and phosphorylation products; ATP production (substrate level and oxidative phosphorylation, photophosphorylation, C3, C4); coupling reactions; uncoupling agents.
BCMB 302 CELL BIOLOGY II 2 Credits
Cell Surface and Communication: Extracellular matrix (including cell walls), Cell adhesion and junctions, Signal transduction, Receptor function, Excitable membrane systems.
Cytoskeleton, Motility, and Shape: Actin-based systems (including muscle contraction), Microtubule-based systems, Intermediate filaments, Prokaryotic systems;
Protein Synthesis and Processing: Regulation of translation, Post-translational modification, Intracellular trafficking, Secretion and endocytosis.
Cells as organisms: bacteria life cycles, protozoa and algae, parasitic protozoa and fungi as free-living and parasitic organisms.
BCMB 303 MOLECULAR BIOLOGY I 2 Credits
Purine and pyrimidine biosynthesis: Regulation of biosynthesis. Structure and properties of nucleosides and nucleotides. Biosynthesis of deoxyribonucleotides; thymidylate biosynthesis. Salvage pathways.
DNA and chromosome structure: Evidence for DNA as carrier of genetic information. Primary and secondary (A, B and Z DNA) and tertiary structure of DNA. Elucidation of DNA structure. Watson and Crick double helix. Structural differences between RNA and DNA. Methods for sequencing DNA. Organisation of DNA in chromosomes, nucleosome structure.
DNA replication: Mechanism of replication (prokaryotic and eukaryotic). Evidence for semi-conservative replication. DNA replicating enzymes. Directionality of replication.
Transcription: Mechanism of transcription (prokaryotic and eukaryotic). Features of a typical transcription unit. Characteristics of different types of RNA. Modification and processing RNA. Reverse transcription.
BCMB 304 MOLECULAR BIOLOGY II 2 Credits
The genetic code: Deciphering the code. Universality and degeneracy of the genetic code. Wobble hypothesis, colinearity of gene polypeptide.
Translation: Ribosome structure. Activation of Amino acids. Initiation, elongation and termination. Eukaryotic and prokaryotic. Post-translational modifications; Polysomes, inhibitors of protein synthesis.
Control of gene expression: Inducible and repressible operons, (lac and trp operons).
Mutation: molecular basis of mutation. Point mutation – transitions, transversions, frameshift mutations. Site-directed mutagenesis, Radiation induced mutation. Chemically induced mutation. DNA repair mechanisms.
Recombinant DNA and genetic engineering: Restriction endonucleases, Methods for recombinant DNA production, transformation, amplification, screening for cloned DNA.
BCMB 305 BIOCHEMISTRY OF HORMONES 2 Credits
General introduction: Coordination in multicellular organisms
Major classes of hormones: Mammalian, plants, insects.
Major endocrine glands: Hypothalamus, pituitary, adrenals, testes, ovaries, pancreas.
Biosynthesis and degradation of hormones: regulation of synthesis/secretion; major biochemical effects and actions.
Hormone receptors: structure, relationship to binding to response, binding characteristics, segregation, auto-phosphorylation/cross-phosphorylation; internalization.
Types of post receptor mechanism: second messenger generation, hormone response elements, gene expression.
BCMB 306 INTEGRATION AND CONTROL OF METABOLISM 3 Credits
Metabolic control: Design of metabolic pathways. Regulatory enzymes fine control (allosteric, substrate/product feed- back and feed-forward controls, covalent modification) and coarse control (induction and repression of enzyme synthesis).
Regulation of fuel metabolism: glycolysis, gluconeogenesis, glyceroneogenesis, glycogenolysis and glycogenesis, Krebs cycle, lipogenesis and lipolysis, β-oxidation, ketogenesis, amino acid metabolism. Role of hormones (e. g. insulin, glucagon, epinephrine) and DNA binding proteins (e. g. Cyclic AMP response element binding protein (CREB), Carbohydrate response element binding protein (ChREBP), Sterol regulatory element binding protein (STREB)).
Integration of metabolism: Glucose homeostasis and glucose transpoters. Interrelationships between carbohydrate, lipid, and protein metabolism. Enzyme profiles of tissues and organs. Interorgan relationships (liver, brain, muscle, adipose tissue) in different physiological states: e. g. Fed, fasted, running athlete and pregnancy.
BCMB 307 DATA HANDLING & INTERPRETATION 1 Credit
Data types; Discrete and ordinate data.
Simple definitions and Descriptive Statistics; mean, standard deviation, standard error of mean etc.
Statistical principles: Importance of statistics; sampling from populations; Gaussian and non-Gaussian distributions; confidence intervals; p-value; statistical significance; statistical power; Baysian perspective on interpreting statistical significance;
Data presentation tools: Tables, graphical types such as histograms, scatter plots, bar graphs, box plots etc
Data analysis: Multiple comparisons; analysis of one group; analysis of two or more groups; Analysis of variant (ANOVA); Analysis of survival data; Categorical data (contingency tables); odds ratios and proportions tests; correlation and linear regression; choosing the right statistical test.
Experimental Design: Response variables (measurements of interest); factors or treatments (influencing variables); number of replicates; type of randomization; time and place of the measurements; sources of error.
Statistical packages and their applications: Excel, Minitab etc.
BCMB 308 BIOENERGETICS 2 Credits
Overview of chemical thermodynamics: Internal, energy, enthalpy, entropy, Gibb’s free energy, laws of thermodynamics; Spontaneous and non-spontaneous processes; Free energy changes in biochemistry.
Principles of thermodynamics and their application to the energetics of the cell: Redox systems, electron donors and acceptors, redox couples, redox potentials, electromotive force, protonmotive forces.
The concept of high energy compounds: phosphoric acid anhydrides, phosphoric-carboxylic acid anhydrides, phosphoguanidines, enolphosphates and thiol esters; basis for the high standard free energy of hydrolysis; the central role of ATP; (phosphate) group transfer potentials; substrate-level phosphorylation; energetics of coupled reactions.
ATP synthesis: review of structure of mitochondrion and chloroplast; sources of energy; redox complexes for electron transport in mitochondria and in chloroplasts; establishment of proton gradients; coupling of ATP synthesis to dissipation of proton gradient; H+ -ATPase; couplers (thermogenesis). ATP utilization for the performance of cellular work; active membrane transport and mechanical work such as muscle contraction.
BCMB 309 PRINCIPLES OF LAB ORGANIZATION & MANAGEMENT 2 Credits
Principles of Laboratory Management: Organisational structure: concepts and models; Principles of Leadership: Past, Present, and Future; Management Functions; Managerial Problem Solving and Decision Making.
Human Resource Management: Human Resource Guidelines and Regulations; Job Analysis, Work Descriptions, and Work Groups; Supervision; Performance Evaluation and Professional Development.
Financial Management: Fundamentals of Financial Management; Effective Budgeting in the Laboratory; Cost/Benefit Analysis (Costing of Services; Justification for Introduction/ Continuation/ Discontinuation of a Service; Lease or Purchase decision analysis).
Operations: Laboratory design for different types and sizes of institutions (selection of equipment and systems, concepts of workstation consolidation, work flow analysis, concepts in laboratory automation [sample transportation systems, modular systems, robotics]); Procurement and Inventory Control; Work load statistics; Staffing; Personnel training and development; Equipment and facilities maintenance planning; Marketing Concepts. Public Relations.
General Principles of Quality Assurance and Quality Control: Introduction to Quality Assurance; Quality Management System, Quality Assurance (QA) and Quality Control (QC); Compliance/Regulations Issues: Laboratory Standards and their Main Features (ISO 9001, ISO/IEC 17025 and ISO 15189), Good Laboratory Practice (GLP).
Ethical Issues in Laboratory Management
BCMB 311 PRACTICAL BIOCHEMISTRY II 3 Credits
- Enzyme catalysed reactions: Time course of reaction; effects of various factors on reaction rate: enzyme concentration, pH, temperature, substrate concentration, activators and inhibitors; enzyme specificity; protease activity in plant extracts; purification of enzymes from plant juice; use of enzyme as an analytical tool (e.g. Estimation of urea in urine).
- Mini project: Isolation, purification and characterisation of a known enzyme.
BCMB 312 CELL & MOLECULAR BIOLOGY PRACTICAL I 3 Credits
Preparation of microbial cells: Safety precautions; sterility; types of growth media (liquid, solid); identification and classification of microorganisms: morphology, Gram stain, biochemical tests; measurement of microbial concentrations; comparison of growth rate in differently constituted media; selective action of antibiotics.
Cell fractionation: Cytoplasm, Nuclear, Mitochondria, Mitoplast; Assay for enzyme markers e.g. succinate dehydrogenase.
Use of protein assay to monitor cell growth: Cell growth; cell density; centrifugation; protein determination.
Cell Behaviour: Cell interactions; kinetics of cell pairing; phagocytosis; kinetics of phagocytosis; exocytosis.
DNA technology: Isolation, purification and manipulation of DNA; RFLP, PCR, Hybridization.
BCMB 313 BIOCHEMISTRY OF VIRUSES 2 Credit
Viruses: Classification; particle structure and stability; the virus genomes; virus replication, cell to cell movement; virus genetics; virus transmission; virus-host interactions. Tools of virus research: electron microscopy, serology and immunochemistry, molecular methods (hybridization, PCR and RT-PCR). Virus epidemiology and control. Plant viruses (cocoa swollen shoot virus), animal viruses (HIV, bird flu virus) and bacterial viruses (Bacteriophages).
BCMB 314 MEMBRANE BIOCHEMISTRY 2 Credits
Introduction: Membrane types and functions; chemical composition (lipids, proteins and carbohydrates); amphipatic nature of lipids (formation of monolayers, bilayers/liposomes, and micelles); Reactions of phospholipases.
Structure and properties: Models (Dawson and Danielli, Singer and Nicholson); integral (glycophorin A, anion channel ban 3, bacteriorhodopsin), lipid-anchored and peripheral (cytoskeleton of erythroid and non-erythroid cells) proteins; plasma membrane glycocalyx, antigenic properties (RBC M and N, blood group O, A and B); evidence for asymmetric, dynamic and fluid-like character of biomembranes; cell-cell recognition and fusion (eg flu virus and HIV infections); membrane biogenesis (synthesis and transport of membrane lipids).
Preparation and study: Physical, chemical and biochemical methods of study (lipid bilayer and vesicles of eukaryotic and prokaryotic cells).
Transport: Thermodynamics; modes (uniport, symport and antiport systems) and types (simple diffusion, passive-mediated, active, Na/K pump, co-tranport – Na/glucose pump of kidney/intestine, galactose permease of E. coli, exocytosis and endocytosis); channels (ligand gated and voltage-gated) and pores; ionophores (valinomycin, gramicidin A and nigericin).
BCMB 316 INDUSTRIAL MICROBIOLOGY 2 Credits
Introduction: Importance and effects of microorganisms in industry, Nature of industrial microbiology, microorganism of industrial importance; Mutation, strain selection and development, hybridisation; media formulation and economic; optimisation of fermentation media at laboratory scale, perimeter design operation; Antifoams; aspects of biochemical engineering; patents and patent law.
Microbial contamination in industry: Microbial contamination in industry, Regulatory and advisory bodies, Microbiology testing programs, Quality control;
Microbial biotechnology: Properties of an industrial microorganism, growth factors and conditions of industrial microorganisms, Product formation, Aspects of the biology of moulds, yeasts, bacteria, actinomycetes and viruses of importance in various fermentation. Culture techniques and maintenance of selected cultures, Application of modern techniques of genetics and physiology to the large-scale production of microbial products; industrial strain improvement; scale-up of microbial processes; survey of industrial processes using microorganisms.
Industrial processes: Production of pharmaceutical compounds, commercially valuable non-pharmaceutical compounds, food and food supplements. Pollution control.
BCMB 400 RESEARCH PROJECT 6 Credits
Research project covering a range of subjects utilizing biochemical principles, analytical, cell and molecular biology techniques, demonstrating candidates’ ability to identify original subjects for research, plan, execute and report in seminars and a thesis.
BCMB 401 PROTEIN CHEMISTRY I 2 Credits
Primary structure: amino acid composition of proteins, determination of amino acid sequence, importance of primary structure synthesis of peptides, covalent modification of polypeptides.
Secondary structure (regular arrangement of the polypeptide backbone): peptide bond and its structural implications; random polymers; Ramachandran Plot. Regular conformation of polypeptides; a-helix, b-pleated sheets, other helices (310- helix), super-secondary structures (coiled-coil a-helix). Examples: fibrous proteins; a-keratins, silk fibroin, collagen.
Tertiary structure (folded conformation of globular proteins): determination of protein structure by X-ray crystallography, evidence for folding, reverse turns (b-turns) super-secondary structures (motifs), domains, interiors and exteriors, unfolding and folding. Example: Myoglobin.
Quaternary structure (aggregation of globular proteins). Example: haemoglobin.
Physical forces responsible for maintaining structure.
BCMB 402 PROTEIN CHEMISTRY II 2 Credits
Protein-ligand Interactions: Binding sites of haemoglobin and myoglobin, binding of oxygen and carbon monoxide, micro-environment of the haem iron, the Hill Plot. Protein engineering.
Allostery: interaction between binding sites. Theoretical models; the Mond-Wyman-Changeux (MWC) concerted mechanism, the Koshland-Nemethy-Filmer (KNF) sequential model. Allosteric properties of haemoglobin; molecular mechanism of cooperative binding of oxygen to haemoglobin, the Bohr effect, binding of 2, 3-bisphosphoglycerate (BPG).
Mechanism of Enzyme Catalysis: General acid-base catalysis and covalent catalysis. Catalysis by coenzymes; pyridoxal phosphate, thiamine pyrophosphate, ATP, coenzyme A, NAD(P)+ , FAD/FMN. Structure and mechanism of action of selected enzymes. Examples; dehydrogenases, proteases, ribonuclease, lysozyme, glycolytic enzymes such as phosphofructokinase (PFK).
BCMB 403 MOLECULAR BIOTECHNOLOGY & APPLICATIONS 2 Credits
Tools of molecular biology: Agarose and polyacrylamide gel electrophoresis; Northern and Southern blots and hybridization analysis; Western blots and protein detection; PCR and RAPD, RFLP.
Purification and characterization of nucleic acids: Principles for extraction and purification; concentration and molecular weight determination; species differentiation (RNA/DNA, single/double stranded nucleic acids).
Modifying enzymes: Restriction endonucleases; other nucleases (DNAse, RNAse); ligases; polymerases.
Recombinant DNA technology: Cloning and expression vectors, recombinant molecules and transformation systems (prokaryotic and eukaryotic hosts); colony screening, plasmid isolation and characterisation; transduction and conjugation.
Nucleotide sequencing and mutagenesis: Sequencing of end labelled DNA by base specific chemical cleavage (Maxam and Gilbert) and analysis of primed enzymatic synthesis (Sanger); deletion and insertion mutagenesis.
Gene expression detection: principles of RT-PCR, real time RT-PCR, microarrays.
- Applications: medicine, agriculture and industry.
BCMB 404 IMMUNOLOGY AND IMMUNOCHEMISTRY 2 Credits
Defense systems: self and non-self; innate and acquired; cells and organs involved; humoral and cell-mediated.
Antigens: Immunogenicity and antigenicity; chemical nature (bacterial, viral and synthetic)
Antibodies: Structure and function of immunoglobulins; theories of antibody production; polyclonal antibody production; monoclonal antibody production (hybridoma Technology).
Antigen-antibody interactions: Agglutination and precipitation; immunoassays.
The complement system: components, activation (classical and alternative
Vaccines: Current methods for development. Immune regulation and tolerance; immunopathology (hypersensitivity, immunodeficiency, autoimmunity); transplantation immunology (mechanisms involved in tissue rejection).
Cytokines: General properties; biological activities of selected cytokines.
Immunology of diseases of public health interest: HIV/AIDS, Malaria, Schistosomiasis.
BCMB 405 CELL SIGNALLING 2 Credits
Types of cellular regulation: endocrine, paracrine, autocrine, direct cell-to-cell communication
Primary signalling molecules: growth factors, hormones, neurotransmitters
Structure and properties of receptors: Cell surface and intracellular receptors, G-protein coupled receptors, receptor tyrosine kinases. Conserved domains, ligand recognition, binding characteristics, receptor dimerization and phosphorylation, docking sites and substrate interactions.
Guanine nucleotide binding-protein switches: Heterotrimeric and monomeric, G-protein regulators - GTPase activating proteins and guanine nucleotide exchange factors e.g. Son of sevenless, neurofibromin.
Second messenger generation: cyclic AMP, cyclic GMP, inositol trisphosphate, diacylglycerol, Ca2+
Examples of major cascades: Ras-mitogen activated protein kinase pathway, phosphatidylinositol-3-kinase and Akt pathway, Janus kinase and Signal transducer and Activator of Transcription pathway (JAK-STAT), Nitric oxide-guanylyl cyclase signaling. Effectors, transcription factors, amplification, signal diversity, cross-talk and signal termination.
BCMB 406 MOLECULAR GENETICS 2 Credits
Genetic Foundations: Overview of Mendelian and non-Mendelian inheritance, Transformation, transduction, and conjugation, Recombination and complementation, Mutational analysis, Genetic mapping and linkage, Analysis.
Chromatin and Chromosomes: Overview of Karyotypes, Translocations, inversions, deletions, and duplications, Aneuploidy and polyploidy Structure.
Genomics: Genome structure, Physical mapping, Repeated DNA and gene families, Gene identification, Transposable elements,
Genome Maintenance: DNA replication, DNA damage and repair, DNA modification, DNA recombination and gene conversion.
Gene Regulation in Eukaryotes: Cis-acting regulatory elements, Trans-acting regulatory factors, Gene rearrangements and amplifications, Genetic manipulation of bacteria: transposons and plasmids. Large scale genome analysis: the human genome project.
BCMB 407 CELL & MOLECULAR BIOLOGY PRACTICAL II 3 Credits
Cell Biology: Preparation of Cytoskeleton: Reactivation of Ciliary Beat; Cytoskeletal transformation e.g of sea urchins coelomocyles: Induction of Shape Change via Hypotonic Shock; Effect of Colchicine on Coelomocyte Cell Shape Changes; Effect of Ca2+ and Ca2+ ionophore on Shape Changes of Coelomocytes. Preparation of lymphocytes
DNA technology: Isolation, purification and manipulation of DNA; transformation and screening.
BCMB 408 ENTREPRENEURSHIP FOR INNOVATIONS IN BIOSCIENCES 2 Credits
General Principles of Entrepreneurship: Nature and Importance; The Individual Entrepreneur; Technology Entrepreneurism; Characteristics of Successful Technology Based Businesses; Technical Risk Assessment; Alternative Technology Assessment; Entrepreneurial Process; Entrepreneurial Decision Making; Creativity and the Business Idea; Product Planning and Development System; Resource Needs; Alternative Financing Models; Intellectual Property Protection; Patents, Trademarks, and Copyright in Technology Venturing; Preparing for Venture Launch; Managing Growth and Expansion.
Innovation in Biosciences: Medicine (Diagnosis, Therapeutics, etc); Food & Agriculture (Quality, Safety, Production Efficiency and Processing); Environment (Remediation, Conservation and Restoration); Value added Natural Products;
BCMB 409 BIOCHEMISTRY OF PARASITES 2 Credits
Pathophysiology of the following tropical parasitic diseases: Malaria, trypanosomiasis, filarasis, schistosomiasis and gastrointestinal worm infestations. Biochemistry of the causative parasites with emphasis on host-parasite interrelationships: Molecular basis of chemotherapeutic attack of parasites.
BCMB 410 SEMINARS AND SCIENTIFIC WRITING (Continuous assessment) 1 Credit
Review of language structure and usage.
Types of scientific reports: Seminars, research papers, proposals, posters.
Structure of scientific reports: Title, authors, abstract/summary, Table of content, Glossary; Introuction (context, focus, justification); Materials and Methods; Results; Discussion; Conclusion; References; Appendixes.
Writing style and Rules: Dos and Don’ts; Plagiarism.
In addition, students are required to attend all departmental seminars, (presented by either internal or external speakers), present journal articles (journal club), research proposal and project seminars.
BCMB 411 CLINICAL BIOCHEMISTRY 2 Credits
Introductory practical clinical biochemistry: Laboratory investigations; specimen collection, analytical methods and standardization (calibration standards, precision, accuracy, sensitivity, specificity etc); review of analytical and separation methods used in clinical biochemistry for metabolites, ions and enzymes; report and result interpretation; reference values and factors affecting them.
Organ function disorders and tests: gastrointestinal, liver, kidney, heart, pituitary, pancreas, thyroid, adrenal and gonadal.
Body fluid composition and abnormalities: water and electrolyte balance, acid-base disorders and O2 transport.
Disorders of metabolism (in-born errors of metabolism): lipids, carbohydrates, amino acids, proteins, purines and porphyrins.
Industrial visits to Clinical Laboratories.
BCMB 414 PLANT BIOCHEMISTRY 2 Credits
Carbohydrates: germination of seeds with carbohyrate stores; storage carbohydrates (starch, sucrose and other reserve carbohydrates); structural carbohydrates (cellulose, hemicellulose, pectin); the biosynthesis of carbohydrates.
Lipids: germination of oil seeds, the glyoxalate pathway and gluconeogenesis; chemistry of plant lipids: cutins, suberins and waxes; fatty acid biosynthesis.
Nitrogen metabolism: nitrogen fixation (dinitrogenase); nitrogen uptake and reduction.
Secondary metabolites: Terpenes (the mevalonic acid pathway); phenolic compounds (the shikimic acid pathway); saponins, cardiac glycosides, cyanogenic glycosides and glucosinades and alkaloids; functions
Photosythesis: Chloroplast structure; photoreceptors and transduction of light into chemical energy (the photosynthesis electron transport chain); carbon fixation; the C3, C2 and C4 cycles; CAM metabolism.
Molecular and biochemical regulation of plant metabolic pathways activated in response to environmental cues: environmental stress, and interaction with pathogenic and symbiotic organisms.
Cell wall formation (primary wall, wood), secondary metabolism (lignin, flavonoids, phenolics), wounding, plant defenses (phytoalexins, oxidative burst, hypersensitivity), responses to drought, flooding, salinity, pollutants (heavy metals, ozones).
BCMB 415 XENOBIOTIC METABOLISM 2 Credits
Pathways of xenobiotic metabolism; Phase I and II reactions. Enzymology and molecular mechanisms of xenobiotic metabolism; cytochrome P-450-dependent mixed-function oxidation reactions, microsomal flavin-containing monooxygenases, prostaglandin synthetase, reduction enzymes, epoxide hydrolase and conjugating enzymes. Factors affecting xenobiotic metabolism; internal and external. Pharmacological and toxicological aspects of xenobiotic metabolism - Pharmacological; activation and deactivation, changes in pharmacological response, drug uptake and distribution, enterohepatic circulation. Toxicological; metabolic activation (increased toxicity) - carcinogenesis, mutagenesis, teratogenesis, pulmonary, hepatic and renal toxicities. Deactivation (decreased toxicity). Balance between toxification and detoxifying pathways.
BCMB 416 BIOREMEDIATION 2 Credits
Review of bacterial genetics and genomics. Microbial diversity, distribution and detection in the environment.
Microbial responses to environmental changes: Direct physical and chemical effects, fine control, coarse control, morphological & genotypic changes.
Biochemical cycling of C; N; S, Fe, Hg.
Molecular mechanisms: Selected biochemical pathways in microbes involving Oxygenases and Peroxidases, microbial dechlorination reactions.
Biodegradationof aromatic, aliphatic chlorinated and non-chlorinated hydrocarbons;Polymer metabolism (eg. cellulose, xylan or pectin).
Environmental Applications: Replacement of Petroleum Products; Bio-fuels, Industrial Bio products
Prevention and Management of Environmental Contamination: Sewage Treatment, Bio-leaching, Biodegradable Materials.
Introduction to Phytoremediation.
BCMB 418 INSECT BIOCHEMISTRY & CHEMICAL ECOLOGY 2 Credits
Distinctive nature of insect metabolism: Energy metabolism; synthesis; storage mobilization; transport and utilization of fuels in flight; regulatory factors.
Insect hormones affecting growth and development: Biochemical activities; insect growth regulators. Insect control: Insecticides and their modes of action; detoxification mechanisms; insecticide resistance, synergists; new approaches to insect control.
Chemical ecology: Plant adaptation to environment; chemistry of pollution; plant-insect interactions (insect feeding stimulants, repellents, chemistry of plant defence); animal-animal relationships; pheromones; plant-plant relationships; plant-microorganism relationship-phytoalexins