Medical University of Bialystok. News.
  • Updated 29.04.2024 by Zakład Biochemii Lekarskiej

    News

    The biochemistry lectures will be on May 13th and 20th. 
    The last one will contain information about biochemistry exam.

     

    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       friday     9:00 - 10:00
    Tomasz Gogiel       friday     9:00 - 10:00
    Lech Romanowicz  friday     9:00 - 10:00
    Anna Tokarzewicz  friday     9:00 - 10:00

     

    Biochemistry exam information

    First term – June 14th, 8:20 am.

    Collegium Universum lecture hall

     

    Retake terms:

    1. September 3rd, 8:20 am.

    Collegium Universum lecture hall

     

    2. September 12th, 8:20 am.

    Collegium Universum lecture hall

     

    All other information will be presented on the last lecture.

     

     

    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), collagen triple helix;

    Inborn defects in protein structure - hemoglobin

    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

    Synthesis of triacylglycerols

    Obesity

    Ketone bodies (with structures)

    Ketone bodies – synthesis and degradation

    Phospholipids: glycerophospholipids, sphingolipids

    - structure, properties, synthesis and degradation;

    Blood group antigens

    Steroids: cholesterol (with structure), bile acids;

    Synthesis of cholesterol

    Lipoprotein complexes in human plasma

    Disorders of lipid metabolism

     

    Biochemical calculation

     

     

    Credit III

     

    Protein and amino acid metabolism

    Metabolism of amino acids
    Pool of free amino acids
    Degradation of proteins in alimentary tract
    Degradation of intracellular and extracellular proteins
    Amino acid synthesis
    Transamination
    Deamination of amino acids by dehydrogenases, oxidases and specific deaminating enzymes
    Urea cycle (with structures)
    Defects of urea synthesis

    Glutamine synthesis and cleavage

    Glucogenic amino acids: Ala, Asp, Glu, His;

    Ketogenic amino acids: Leu, (Lys);

    Gluco-ketogenic amino acids: Phe and Tyr;

    Inborn defects in amino acid metabolism: phenyloketonuria, tyrosinemia, alkaptonuria;

    Alternative pathways of Phe and Tyr catabolism

    Amino acids as substrate in synthesis of various biomolecules:

    Active formate, active methyl group:

    formyl-tetrahydrofolate (formyl-THF), S­adenosylmethionine (SAM);

    Catecholamines – synthesis,

    Thyroid hormones,

    Nicotinamide, taurine, active sulphate,

    Serine – homocysteine – cysteine conversion (transsulphurylation),

    Gamma-aminobutyrate, histamine, taurine, putrescine, polyamines,

    Synthesis of creatine, phosphocreatine, NO;

     

    Seminar 3

     

    Vitamins soluble in water: B1, B2, B3, B5,

    B6, B7, B9, B12, C;

    Vitamins soluble in lipids: A, D, E, K;

     

    Micronutrients:

    iron, zinc, copper, manganese, iodine;

     

    Ethanol metabolism

     

    Oxidation of ethanol

    Metabolism dysregulation by ethanol

    Toxic effects of acetaldehyde

     

    Energy metabolism specificity of different organs

     

    Liver, skeletal muscle, heart muscle, kidney, brain, fat tissue

     

    Porphyrins

     

    Heme, chlorophyll, vitamin B12

    Heme synthesis and degradation

    Bile pigments (bilirubin, biliverdine)

    Jaundices

     

    Metabolism of nucleotides

     

    Purine and pyrimidine bases, nucleosides, nucleotides

    -structures, names, symbols, basic and rare ones;

    Atypical nucleotides: NAD, NADP, FMN, FAD;

    Degradation of: purine nucleotides, nucleosides,

    Degradation of: pyrimidine nucleotides, nucleosides, bases;

    Synthesis of purine and pyrimidine nucleotides

    Salvage pathways of nucleotides’ synthesis

    Synthesis of deoxyribonucleotides

    Synthesis of NAD, FMN, FAD;

    Disorders of nucleotides’ metabolism

     

    Credit IV

     

    Metabolism of nucleic acids – part I

     

    Nucleic acids: DNA and RNA – differences in composition;
    Primary structure of DNA: phosphodiester bonds, 3’ and 5’ end;
    Double helix structure
    Denaturation and renaturation of DNA
    Viscosity change during DNA denaturation
    Hyperchromicity of DNA denaturation
    Chromatin structure:
    Histones, nucleosome, chromatosome,
    DNA grooves;

    Ribonucleic acids: mRNA, tRNA, rRNA, RNA regulatory molecules;
    Genetic code/amino acid code
    DNA replication in prokaryotes and eukaryotes
    Telomerase

    DNA damage and repair

    Common and specific properties of DNA polymerases

    Polymerase Chain Reaction

     

    Metabolism of nucleic acids – part II

     

    Transcription in prokaryotes and eukaryotes (similarities and differences)

    Posttranscriptional modifications of RNAs in prokaryotes and eukaryotes

    Protein synthesis:

    Formation of aminoacyl-AMP and aminoacyl-tRNA,

    Initiation, elongation, termination

    Translation in eukaryotes

    Posttranslational modifications of proteins

    Inhibition of protein synthesis

    Sorting proteins

    Gene expression (prokaryote, eukaryote)

    Mutations

    Human genome

    Recombination of DNA

    Genetic engineering

    Stem cells

     

     

    Hormones

     

    Definition, classification;

    Peptide hormones:

    Insulin – structure, synthesis, regulatory functions of;

    Insulin influence on glucose metabolism:

    on transport to the cell, glycolysis, gluconeogenesis, glycogenesis, glycogenolysis;

    Insulin influence on lipolysis, lipogenesis, protein synthesis;

    Glucagon – regulatory functions of;

    Hormones - amino acid derivatives:

    Thyroid hormones,

    Catecholamines;

    Steroid hormones:

    Mineralocorticoids,

    Glucocorticoids,

    Estrogens, gestagens, androgens;

    Mechanism of insulin action on the cell – insulin receptor

    Second messengers: cAMP, cGMP, Ca2+, DAG, IP3, NO; formation, inactivation;

    Mechanism of hormone action through the receptors: membrane, cytosolic, nuclear;

    Calcium metabolism

     

    Cytokines

     

    Peptide growth factors

    Interleukins

    Interferons

    Tumor necrosis factors

    Eicosanoids: prostaglandins,

    thromboxanes, leukotrienes

     

     

    Transport through biological membranes

     

    Biological membranes

    Passive and active transport

    Gap junctions

    Ion channels

    Transport of sugars and amino acids

    Na+/K+ pump

    H+/K+ pump

    Calcium transport

    Facilitated diffusion

    Transport of reducing equivalents through inner mitochondrial membrane

    Transport of fatty acids from cytosol to mitochondrion

    Transport of acetate from mitochondrion to cytosol

    Transport of macromolecules across biological membranes

     

     

    ----------- Additional subjects for exam

     

    Integration and regulation of metabolism

     

    Metabolism, catabolism, anabolism

    Metabolism regulation through: metabolic signals, feedback inhibition, neurotransmitters receptors

    Metabolism integration - glucose homeostasis

     

    Diabetes

     

    Seminar 5

     

    Macronutriens:

    sodium, potassium, calcium, magnesium, chlorine, phosphorus;

     

    Xenobiotics

    Mechanisms of xenobiotic action

    Biotransformation