Biology: Blood and Oxygen Transport
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Questions and Answers

Fatty acids may perform a lot of functions excluding:

  • Plasticity (synthetic)
  • Structural components of complex lipids
  • Energy production (correct)
  • Structural components of cell membranes

    • Main function of glycosphingolipids is:

  • Sources of energy for cells
  • Body heat loss prevention
  • Components of cellular membranes (correct)
  • Storage

    • What is true as a description of chylomicrons:

  • The lack of a part of triacylglycerols is a result of hepatic triacylglycerol lipase activity
  • They have the largest diameter among all lipoproteins (correct)
  • Main lipid constituent is cholesterol
  • Main apoprotein is apoB100

    • Transport of exogenous lipids from intestine to tissues is provided by:

    <p>Chylomicrons</p> Signup and view all the answers

    Main function of glycerophospholipids is:

    <p>Components of cellular membranes</p> Signup and view all the answers

    ATP in red blood cells is used mainly for...

    <p>Active transport</p> Signup and view all the answers

    Choose a variant of Hb which cannot transport oxygen in blood.

    <p>MetHb</p> Signup and view all the answers

    Increase of affinity and rate of O2 binding to Hb is a result of...

    <p>Positive cooperative effect</p> Signup and view all the answers

    Choose a pathologic variant of Hb appearing due to mutations in gene coding β-chain of Hb.

    <p>HbS</p> Signup and view all the answers

    If total protein concentration in patient’s plasma is 78 g/l, it means...

    <p>Hypoproteinemia</p> Signup and view all the answers

    Diagnosis of acute viral hepatitis may be estimated by determination of activity of which enzyme?

    <p>Gamma-glutamyltranspeptidase</p> Signup and view all the answers

    Diagnosis of acute pancreatitis may be estimated by determination of activity of which enzyme?

    <p>Amylase</p> Signup and view all the answers

    Which enzyme catalyzes aerobic dehydrogenation, a variant of oxidation reaction?

    <p>Cytochrome oxidase</p> Signup and view all the answers

    In dehydrogenation reactions, what is removed from the substrate?

    <p>Hydrogen atoms</p> Signup and view all the answers

    What significant role do monooxygenases play?

    <p>Xenobiotics detoxification</p> Signup and view all the answers

    What is the caloric coefficient for carbohydrates?

    <p>4,1 kcal/g</p> Signup and view all the answers

    Which monomers are in the structure of RNA?

    <p>AMP; GMP; CMP; UMP</p> Signup and view all the answers

    Which monomers are in the structure of DNA?

    <p>dAMP; dGMP; dCMP; dTMP</p> Signup and view all the answers

    Which nucleotides can be used in DNA biosynthesis?

    <p>dAMP; dGMP; dCMP; dTMP</p> Signup and view all the answers

    Which nucleotides can be used in RNA biosynthesis?

    <p>AMP; GMP; CMP; UMP</p> Signup and view all the answers

    The bond between nucleotides in the primary structure of nucleic acid is?

    <p>5’,3’-phosphodiester bond</p> Signup and view all the answers

    What stabilizes the secondary structure of DNA?

    <p>Hydrogen bonds</p> Signup and view all the answers

    Choose tetrapeptide which has TWO amino acid residues with hydrophobic side chain:

    <p>Trp-Ile-Cys-Val</p> Signup and view all the answers

    Choose tetrapeptide which has THREE amino acid residues with hydrophilic side chain:

    <p>Asp-Gln-Val-Glu</p> Signup and view all the answers

    Choose tetrapeptide which has N-terminal amino acid residue with hydrophobic side chain:

    <p>Phe-Tyr-Lys-Val</p> Signup and view all the answers

    Choose tetrapeptide which has TWO amino acid residues with hydrophilic side chain:

    <p>Ile-Cys-His-Tyr</p> Signup and view all the answers

    Choose tetrapeptide which has C-terminal amino acid residue with hydrophilic side chain:

    <p>Val-Ser-Tre-Met</p> Signup and view all the answers

    Choose tetrapeptide which has THREE amino acid residues with hydrophilic side chain:

    <p>Ser-Gly-Trp-Pro</p> Signup and view all the answers

    The primary structure in ALL proteins is stabilized with...

    <p>Peptide bonds</p> Signup and view all the answers

    The secondary structure of proteins is stabilized ONLY with...

    <p>Hydrogen bonds</p> Signup and view all the answers

    The tertiary structure of proteins is stabilized with...

    <p>Covalent or/and noncovalent bonds</p> Signup and view all the answers

    The quaternary structure of proteins is stabilized mainly with...

    <p>Noncovalent bonds and hydrophobic interactions</p> Signup and view all the answers

    Indicate a function which is NOT performed by proteins in humans:

    <p>Storing of genetic information</p> Signup and view all the answers

    At neutral pH peptide Asn-Glu-Asp-Val-Phe...

    <p>carries negative charge and is moving towards anode.</p> Signup and view all the answers

    At neutral pH peptide Val-Gly-His-Pro-Arg...

    <p>carries positive charge and is moving towards anode.</p> Signup and view all the answers

    At pH=3 peptide Val-Glu-Phe-Pro-Arg...

    <p>carries positive charge and is moving towards anode.</p> Signup and view all the answers

    At pH=10 peptide Gln-Glu-His-Met-Arg...

    <p>carries positive charge and is moving towards cathode.</p> Signup and view all the answers

    Study Notes

    Here are the study notes for the provided text:

    Protein Structure, Properties, and Functions

    • Primary structure of proteins is stabilized with peptide bonds.
    • Secondary structure of proteins is stabilized ONLY with hydrogen bonds.
    • Tertiary structure of proteins is stabilized with covalent or noncovalent bonds.
    • Quaternary structure of proteins is stabilized mainly with noncovalent bonds and hydrophobic interactions.
    • Functions of proteins in humans:
      • Transport of hormones in blood
      • Muscle contraction
      • Catalysis of reactions
    • Not a function of proteins: Storing of genetic information

    Protein-Ligand Interactions

    • Ligand binding is highly specific and necessary for performing specific biological functions.
    • Examples of protein-ligand interactions:
      • Antigen-antibody interaction
      • Hormone-receptor interaction
      • Protein-heavy metal ion interaction

    Denaturation of Proteins

    • Denaturation is always followed by alterations in its biological function and changes in its solubility.
    • Denaturation can be induced by:
      • Adding a heavy metal salt to a protein aqueous solution
      • Adding a strong acid to a protein aqueous solution
      • Heating a protein aqueous solution

    Vitamins and Enzymes

    • Vitamin B5 (nicotinic acid) is a part of coenzyme NAD.
    • Vitamin B6 is a part of coenzyme pyridoxal phosphate.
    • Vitamin B9 (folic acid) is a part of coenzyme THF.
    • Vitamin B2 (riboflavin) is a part of coenzyme FAD.
    • Vitamin B1 (thiamin) is a part of coenzyme TPP.
    • Vitamin B3 (panthotenic acid) is a part of coenzyme HS-CoA.
    • Functions of enzyme cofactors:
      • FAD: intermediate carrier of hydrogen atoms
      • HS-CoA: intermediate carrier of acyl groups
      • NAD: intermediate carrier of hydrogen atoms
      • THF: intermediate carrier of one-carbon groups
      • Pyridoxal phosphate: intermediate carrier of amino groups
    • Enzyme cofactors and their functions:
      • Pyridoxal phosphate: involved in transamination reactions
      • HS-CoA: involved in acyl transfer reactions
      • NAD: involved in redox reactions
      • THF: involved in one-carbon transfer reactions

    Energy Exchange

    • Aerobic dehydrogenation is catalyzed by cytochrome oxidase.
    • Anaerobic dehydrogenation is catalyzed by succinate dehydrogenase.
    • Dehydrogenation is a type of oxidation reaction in which electrons are removed from the substrate.
    • Functions of monooxygenases:
      • Xenobiotics detoxication
      • Drugs and metabolites inactivation
    • Caloric coefficients for macronutrients:
      • Carbohydrates: 4.1 kcal/g
      • Lipids: 9.3 kcal/g
      • Proteins: 4.1 kcal/g
    • Daily requirements for macronutrients (according to WHO recommendations):
      • Lipids: 4.1 g/kg body weight
      • Proteins: 1 g/kg body weight
      • Carbohydrates: 1.5 g/kg body weight

    Carbohydrates

    • Glycogen is a homopolysaccharide.
    • Sucrose is a disaccharide.
    • Hialuronic acid is a heteropolysaccharide.
    • Galactose is a monosaccharide.
    • Lactose is a disaccharide.
    • Heparin is a heteropolysaccharide.
    • Metabolic pathways:
      • Glycolysis: anaerobic oxidation of glucose
      • Gluconeogenesis: synthesis of glucose from non-carbohydrate substances
      • Pentose phosphate pathway: oxidation of glucose to generate NADPH+H+
      • Glucogenesis: synthesis of glucose from non-carbohydrate substancesHere are the study notes for the text:
    • Carbohydrate Metabolism*

    Gluconeogenesis

    • Located in liver, kidney cortex, and skeletal muscles
    • Inhibitors: insulin, glucose
    • Stimulators: glucagon, cortisol, adrenaline

    Digestion of Carbohydrates

    • Digestion of glycogen and starch in oral cavity catalyzed by amylase
    • Digestion of disaccharides in small intestine catalyzed by sucrase, lactase, and maltase
    • Absorption of sugars in intestinal wall by active transport, facilitated diffusion, and simple diffusion

    Regulation of Blood Glucose Levels

    • Hyperglycemia: blood glucose level > 6.2 mmol/l
    • Hypoglycemia: blood glucose level < 2.8 mmol/l
    • Normal range of blood glucose level in adults: 2.2-4.4 mmol/l
    • Physiologic hyperglycemia: after meal, during physical activity, or emotional stress
    • Pathologic hyperglycemia: diabetes mellitus
    • Physiologic hypoglycemia: starvation, long-term physical activity
    • Pathologic hypoglycemia: overdosage of insulin, Bronze disease
    • Lipid Metabolism*

    Types of Fatty Acids

    • Saturated fatty acids: palmitic, stearic
    • Monounsaturated fatty acids: oleic, palmitoleic
    • Polyunsaturated fatty acids: linoleic, arachidonic

    Functions of Lipids

    • Energy storage
    • Structural components of cell membranes
    • Sources of energy during starvation
    • Can be used as second messengers

    Lipid Transport

    • Exogenous lipids transported from intestine to tissues by chylomicrons
    • Endogenous lipids transported from liver to peripheral tissues by VLDL, IDL, and LDL
    • Reverse transport of cholesterol from peripheral tissues to liver by HDL

    Regulation of Lipid Metabolism

    • Lipolysis in adipose tissue stimulated by glucagon, adrenaline, and cortisol
    • Lipogenesis in adipose tissue stimulated by insulin

    Atherosclerosis

    • Atherogenicity coefficient: (total cholesterol - HDL cholesterol) / HDL cholesterol
    • High risk of atherosclerosis development: atherogenicity coefficient > 3.5
    • Protein and Amino Acid Metabolism*

    Essential Amino Acids

    • Phenylalanine, valine, tryptophan, threonine, isoleucine, methionine, lysine, leucine

    Nitrogen Balance

    • Positive nitrogen balance: during growth, pregnancy, and after surgery
    • Negative nitrogen balance: during starvation, fever, and after trauma
    • Nitrogen equilibrium: during normal adult life

    Transamination Reactions

    • Transfer of amino group from amino acid to ketoacid
    • Cofactor: pyridoxal phosphate

    Urea Cycle

    • Location: liver mitochondria and cytosol
    • Function: detoxification of ammonia
    • Enzymes: carbamoylphosphate synthase I, ornithine transcarbamoylase, arginase

    Biogenic Amines

    • Synthesis: from amino acids
    • Inactivation: by methylation, transamination, and oxidative deamination

    Let me know if you'd like me to continue!### Hormones and their Functions

    • Glucagon is a hormone of the pancreatic gland
    • Tyroxin is a hormone of the thyroid gland
    • Adrenalin is a hormone of the medulla of suprarenal glands
    • Somatotropin is a hormone of the hypothalamus

    Synthesis of Hormones

    • Cortisol, Aldosteron, and Testosteron are synthesised in the cortex of suprarenal glands
    • Somatostatin, Insulin, and Glucagon are synthesised in the pancreatic gland
    • Growth hormone, Thyreotropic hormone, and ACTH are synthesised in the pituitary gland
    • Somatotropin is synthesised in the hypothalamus
    • Calcitonin is synthesised in the thyreoid gland
    • Calcitriol is not synthesised in the thyreoid gland

    Classification of Hormones

    • Hormones of peptide nature include Glucagon, Growth hormone, Insulin, and Thyreotropin
    • Hormones of protein nature include Adrenalin, Thyroxine, Insulin, and Somatotropin
    • Hormones - derivatives of aminoacids - include Adrenalin, Melatonin, T3, and T4
    • Steroid hormones include Aldosteron, Cortisol, Calcitriol, and Testosteron

    Receptors of Hormones

    • Hormones that have receptors in the outer cell membrane include Insulin, Glucagon, and Thyreotropin
    • Hormones that have receptors inside cells (in cytosole or nucleus) include Thyroxine, Cortisol, and Aldosteron
    • Hormones that act on receptors in the nucleus include Thyroxine and Cortisol
    • Hormones that act on receptors in the outer cell membrane include Adrenalin and Glucagon

    Inactivation of Hormones

    • Insulin is inactivated by Oxidative deamination and conjugation
    • Adrenalin is inactivated by Oxidative deamination and methylation
    • Glucagon is inactivated by Oxidative deamination

    Regulation of Metabolic Processes

    • Aldosteron and Vasopressin regulate exchange of water and minerals
    • Testosteron and Estradiol regulate reproductive functions
    • Calcitriol and Calcitonin regulate exchange of calcium and phosphates
    • Glucagon and Cortisol regulate glucose metabolism

    Biochemistry of Blood, Liver, Kidney, and Connective Tissue

    • Erythrocytes lack several metabolic pathways, including protein biosynthesis on ribosomes and DNA replication
    • 2,3-bisphosphoglycerate decreases Hb affinity to oxygen
    • MetHb is a variant of Hb which can not transport oxygen in blood
    • ATP in red blood cells is used mainly for active transport
    • Increase of affinity and rate of O2 binding to Hb is a result of positive cooperative effect

    Kidney and Liver Functions

    • Kidney is the main organ producing Erythropoetin
    • Hepatocytes produce VLDL and HDL
    • Glucokinase in hepatocytes has kinetic properties of high value of Km and is not inhibited by glucose-6-phosphate
    • Direct bilirubin can not be found in urine of patients with hemolytical jaundice

    Connective Tissue

    • Fibronectin is a polydomain protein with main function of integrative
    • Collagen synthesis requires ascorbic acid and produces desmosin after degradation
    • Elastin is a protein responsible for elasticity of tissues and consists of single polypeptide chain
    • Glycosaminoglycans found in extracellular matrix of humans include Chondroitinsulphates, Dermatansulphates, and Keratansulphates

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