Medical University of Bialystok. News.
  • Updated 03.12.2025 by Zakład Biochemii Lekarskiej

    News

    The first lecture will take place on Monday, October 6th at 12:45 in the lecture hall of Collegium Universum, Mickiewicza 2c.

    The biochemistry lectures will be on every Monday, at 12:45, in  Collegium Universum lecture hall.

     

    The laboratory classes will start on Monday, October 6nd at 8:15 am and 2:45 pm (according to dean groups) in laboratories of the Department of Medical Biochemistry (Collegium Universum, 3rd floor).

     

    Please, take with you lab coat, soft footwear and Biochemistry Workbook (can be borrowed in the library or print first class from Biochemistry workbook .pdf version in Recomended handbooks on website of Department of Medical Biochemistry).

     

     

    SEMINARS

    Subjects indicated for self-development;

    They are online on the Blackboard platform.

     

    coordinator: dr hab. Lech Romanowicz

    e-mail: lech.romanowicz@umb.edu.pl
    phone: +48 (85) 748 55 78

     

    consultations:
    Justyna Bączyk      thursday 9:00 - 10:00
    Marta Bruczko-Goralewska       tuesday 12:30 - 13:30
    Tomasz Gogiel       friday     9:00 - 10:00
    Lech Romanowicz  friday     9:00 - 10:00
    Anna Tokarzewicz  friday     9:00 - 10:00

    Katarzyna Miniewska  thursday 9:00 - 10:00

     

    Credit I

    Proteins

    Structure of amino acids

    Classification of amino acids (polarity, charge):

    non-polar: Gly, Ala, Val, Leu, Ile, Phe, Trp, Met, Pro

    polar without charge: Ser, Thr, Tyr, Asn, Cys, Gln

    acidic chains: Asp, Glu

    basic chains: His, Lys, Arg

    Peptide bond

    Nomenclature of peptides

    Biological importance of peptides (with examples)

    Protein structure: I, II (alfa-helix, beta- sheet), III (myoglobin), IV (hemoglobin),

    Inborn defects in protein structure – hemoglobin, collagen

    collagen triple helix;

    Denaturation of proteins

    Properties of proteins in solution (solubility, amphoteric properties, pI)

    Isolation of proteins from biological materials: Column chromatography - size exclusion chr., ion exchange chr., affinity chr., HPLC; PAGE, isoelectric focusing, the Edman reaction

    Protein functions

     

    Enzymology

    Definition of metabolism, anabolism, catabolism

    Equilibrium of chemical reaction

    Activation energy, free energy

    Mechanism of the enzymatic reaction

    Enzyme active site

    Enzymatic reaction velocity and its dependence on: temperature, pH, substrate concentration, allosteric effectors (positive and negative)

    Maximal velocity (Vmax) and Michaelis constant (Km)

    Enzyme activity - units

    Inhibitors

    Proenzymes and their conversion to active forms

    Regulation of enzyme activity

    Multifunctional enzymes on the example of: phosphofructokinase-2,

    fructose 2,6-bisphosphatase, fatty acid synthase

    Multienzyme complexes on the example of:

    pyruvate dehydrogenase, α-ketoglutarate dehydrogenase

    Enzyme specificity

    Coenzymes

    Isoenzymes on the example of: lactate dehydrogenase,

    creatine kinase, malate dehydrogenase, glycerol-3-phosphate dehydrogenase,

    hexokinase

    Classification of enzymes, international enzyme code

    Application of enzymes in medicine and biotechnology:

    markers of disease – aminotransferases

    drugs – asparaginase

    reagents – urease

    gene therapy

     

     

    Bioenergetics

     

    Exergonic reactions and endergonic reactions

    ATP as an energy relay

    High-energy compounds

    Low-energy compounds

    Oxidative phosphorylation

    Substrate phosphorylation

    Mitochondrial respiratory chain

    Respiratory complexes

    Transport of protons and electrons through respiratory chain

    Chemiosmotic theory

    Blocking the respiratory chain

    Uncoupling of oxidative phosphorylation

    Reactive oxygen species

     

    Carbohydrate metabolism

     

    Trioses, tetroses, pentoses, hexoses

    Glucose, mannose, galactose, fructose

    Straight-chain form, cycle form, alpha and beta form

    Aerobic and anaerobic glycolysis (with structures)

    Regulation of glycolysis

    Energy balance of glycolysis

    Oxidative decarboxylation of pyruvate

    Krebs cycle (with structures)

     

     

    Credit II

     

    Gluconeogenesis (with structures)

    Pentose phosphate pathway – course, biological importance

    and connection to glycolysis and gluconeogenesis

    Fructose metabolism and hereditary defects: essential fructosuria, hereditary fructose intolerance

    Galactose metabolism and galactosemias

    Derivatives of simple sugars: glycosides, uronic acids, aminohexoses, sialic acid

    Disaccharides: maltose, isomaltose, sucrose (saccharose), lactose

    Polysaccharides: starch, glycogen

    Biosynthesis and degradation of glycogen

    Regulation of glycogen metabolism

    Inborn defects in glycogen metabolism

     

    Lipids

     

    Fatty acids – saturated and unsaturated;

    Acylglycerols – structure, decomposition;

    Beta-oxidation of saturated fatty acids

    Energy balance of fatty acid oxidation

    Glycerol metabolism

    Synthesis of fatty acids