Medical University of Bialystok. Biochemistry course programme.
  • Updated 17.11.2023 by Zakład Biochemii Lekarskiej

    Biochemistry course programme


    Aim of the course: The programme of teaching concentrates on presentation of those aspects of human biochemistry, which helps students to understand the chemical processes occurring in living cells, extracellular matrix and physiological fluids and pathobiochemical processes, which accompany human pathology.


    Lectures – 50 h 

    Classes – 75 h

    Seminars - 20 h


    SYLABUS - download


    coordinator: dr hab. Lech Romanowicz
    phone: +48 (85) 748 55 78


    The material required for final exam on biochemistry

    A. Proteins

    Structure and properties of peptides and proteins: basic information on protein amino acids, peptide bonds, nomenclature of peptides, biologically active peptides, protein structure, properties of proteins in solutions, isolation of proteins from biological materials, molecular weights of proteins, inborn defects in protein structure (haemoglobin – as an example).

    B. Enzymology

    Structure and general properties of enzymes, mechanism of biocatalysis, active site of enzyme, enzyme : substrate complex, factors affecting the velocity of enzymatic reactions, Michaelis constant, inhibition of enzymes, practical applications of inhibitors, proenzymes and their conversion into enzymes, coenzymes and vitamins, isoenzymes, enzyme systematics, enzyme activity units, systematics of enzymes, international enzymatic code, regulation of enzyme activity (dissociation and association of catalytic and inhibitory subunits, limited proteolysis, phosphorylation and dephosphorylation of enzymatic proteins, allosteric effectors, feedback inhibition). Multifunctional enzymes. Application of enzymes in medicine and biotechnology.

    C. Bioenergetics

    Energetic substrates. mitochondrion as a main place of energy production, structure and function of mitochondrial respiratory chain, substrate phosphorylation, oxidative phosphorylation, reactive oxygen species, macroenergetic compounds, specific features of energetic metabolism in various organs: brain cortex, kidney cortex, liver, skeletal muscle, heart muscle, erythrocytes (red blood cells).

    D. Carbohydrate metabolism

    Glucose metabolism: glycolysis, oxidative and nonoxidative decarboxylation of pyruvate, ethanol and its metabolism, Krebs cycle, pentose phosphate pathway, metabolism of fructose and galactose, aminohexoses, uronic acids, gluconeogenesis, disaccharides and their hydrolysis in gut, inborn defects in metabolism of glycogen, galactose and fructose, disaccharide metabolism, ethanol metabolism and toxicity, pathobiochemistry of diabetes mellitus.

    E. Lipid metabolism

    Basic information on lipid structure: fatty acids, acylglycerols, phospholipids, cholesterol, lipolysis in alimentary tract and in tissues, β-oxidation of fatty acids, glycerol metabolism, biosynthesis of fatty acids, biosynthesis of triacylglycerols, biosynthesis and degradation of phospholipids (lecithin as an example), cholesterol biosynthesis, lipoprotein complexes in human plasma, ketone bodies, inborn hyperlipidaemias and hypolipidaemia, pathobiochemistry of obesity.

    F. Metabolism of nucleotides

    Composition of nucleotides (bases, pentoses, phosphate), nomenclature of nucleosides and nucleotides. Nucleotide degradation, nucleotidases, nucleosidases and nucleoside phosphorylases. Biosynthesis of purine and pyrimidine rings, biosynthesis of deoxyribonucleotides, diphosphonucleotides and triphosphonucleotides, uric acid as a final product of purine degradation, pathobiochemistry of nucleotide metabolism.

    G. Protein and amino acid metabolism

    Degradation of protein in alimentary tract, decarboxylation of amino acids, transamination and deamination, urea cycle, glutamine and asparagine as products of glutamate and aspartate amination, amino acids as substrates in gluconeogenesis and ketogenesis, transsulfurylation. Inborn defects in amino acid
    metabolism: phenyloketonuria, tyrosinemia, alkaptonuria, albinism. Amino acids as substrate in biosynthesis of various biomolecules: other amino acids, amines and polyamines, hormones, pigments, hem, neurotransmitters, purines, pyrimidines, carnitine, phospholipids, etc.

    H. Porphyrines

    Hem, chlorophyll, hem biosynthesis, hem degradation, bilirubin and its derivatives, pathobiochemistry of hem metabolism.

    I. Nucleic acids

    DNA: primary structure, secondary structure. DNA replication. Mutations. Transcription and posttranscriptional modification of RNA. Translation - Protein synthesis. Posttranslational modification of proteins. Gene function. Human genome. DNA recombination.

    I. Transport through biological membranes

    Passive transport, active transport, mediated transport. Structure and localisation of biotransporters. Transport of Na+, K+, Ca2+, Cl-, HCO3-. Transport of glucose and amino acids through the cell membrane. Transport of fatty acids from cytosol to mitochondrion. Transport of acetate from mitochondrion to cytosol. Transport of reducing equivalents through inner mitochondrial membrane.

    J. Extracellular matrix (ECM) biochemistry

    ECM composition: collagen and its molecular polymorphism, specifics of biosynthesis and posttranslational modification, collagenolysis, enzymes of ECM, elastin, fibronectin, laminin, glycosaminoglycans and proteoglycans.

    K. Blood biochemistry – selected topics

    Haemoglobin structure and its role in oxygen transport, factors affecting oxygen binding to haemoglobin, plasma proteins, blood clotting and fibrinolysis.

    L. Metabolism regulation

    Structure of the main hormones. Biosynthesis and inactivation of catecholamines and steroid hormones. Action mechanisms of peptide, amino acid and steroid hormones. Role of second messengers: c3’5’AMP, c3’5’GMP, DAG and IP3. Role of proteins G in signal transduction. Intracellular regulatory mechanisms: ATP/ADP, NADH/NAD+, NADPH/NADP+ ratio, feedback inhibition, allosteric effects, phosphorylation and dephosphorylation of enzymatic proteins.

    M. Xenobiotic metabolism

    General characteristics of xenobiotic and their biological effects. Xenobiotic biotransformation; special role of cytochrome P-450 in this process. Main pathways of detoxication: by glucuronate, sulphate, glutathione and glutamine binding, the role of acetylation and methylation in this process.