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Questions and Answers
Diagnosis of acute viral hepatitis may be estimated by determination of activity of which enzyme?
Diagnosis of acute viral hepatitis may be estimated by determination of activity of which enzyme?
Diagnosis of acute pancreatitis may be estimated by determination of activity of which enzyme?
Diagnosis of acute pancreatitis may be estimated by determination of activity of which enzyme?
Aerobic dehydrogenation is a variant of oxidation reaction, which enzyme catalyzes this reaction?
Aerobic dehydrogenation is a variant of oxidation reaction, which enzyme catalyzes this reaction?
Which type of oxidation reactions involve removal of electrons?
Which type of oxidation reactions involve removal of electrons?
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What significant role do monooxygenases play?
What significant role do monooxygenases play?
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Main function of glycosphingolipids is:
Main function of glycosphingolipids is:
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Main function of glycerophospholipids is:
Main function of glycerophospholipids is:
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What is true as a description of chylomicrons?
What is true as a description of chylomicrons?
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Transport of exogenous lipids from intestine to tissues is provided by…
Transport of exogenous lipids from intestine to tissues is provided by…
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Ketone bodies can be synthesized in…
Ketone bodies can be synthesized in…
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Normal serum concentration range of ketone bodies is…
Normal serum concentration range of ketone bodies is…
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Normal serum concentration range of cholesterol is…
Normal serum concentration range of cholesterol is…
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Normal serum concentration range of free fatty acids is…
Normal serum concentration range of free fatty acids is…
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Normal serum concentration range of total lipids is…
Normal serum concentration range of total lipids is…
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The source of carbon atoms for fatty acids synthesis is…
The source of carbon atoms for fatty acids synthesis is…
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Choose the metabolic pathway in which amino acids cannot be used:
Choose the metabolic pathway in which amino acids cannot be used:
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Choose the urea cycle reaction which is catalyzed by a mitochondrial enzyme:
Choose the urea cycle reaction which is catalyzed by a mitochondrial enzyme:
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Choose the substance that is regenerated in each round of transdeamination reactions:
Choose the substance that is regenerated in each round of transdeamination reactions:
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Methylation (transmethylation) reactions are used for:
Methylation (transmethylation) reactions are used for:
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Deficiency of folic acid and cobalamin may cause:
Deficiency of folic acid and cobalamin may cause:
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Ammonia is toxic due to?
Ammonia is toxic due to?
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Accumulation of arginine in blood is a result of a genetic defect in synthesis of:
Accumulation of arginine in blood is a result of a genetic defect in synthesis of:
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Alkaptonuria is a result of genetic defect in:
Alkaptonuria is a result of genetic defect in:
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Accumulation of argininosuccinate in blood is a result of a genetic defect in synthesis of:
Accumulation of argininosuccinate in blood is a result of a genetic defect in synthesis of:
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Classic variant of phenylketonuria is a result of genetic defect in:
Classic variant of phenylketonuria is a result of genetic defect in:
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Genetic disorder (metabolic disease) hyperammonemia type I is a result of a defect in the:
Genetic disorder (metabolic disease) hyperammonemia type I is a result of a defect in the:
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Functions of serotonin include:
Functions of serotonin include:
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Biogenic amines are inactivated by:
Biogenic amines are inactivated by:
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Functions of adrenaline include:
Functions of adrenaline include:
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Regeneration of methionine from homocysteine requires:
Regeneration of methionine from homocysteine requires:
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Functions of histamine include:
Functions of histamine include:
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The bases which can be found in purine nucleotides are:
The bases which can be found in purine nucleotides are:
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The bases which can be found in pyrimidine nucleotides are:
The bases which can be found in pyrimidine nucleotides are:
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Monomers in the structure of RNA are:
Monomers in the structure of RNA are:
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Monomers in the structure of DNA are:
Monomers in the structure of DNA are:
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Nucleotides which can be used in DNA biosynthesis are:
Nucleotides which can be used in DNA biosynthesis are:
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Nucleotides which can be used in RNA biosynthesis are:
Nucleotides which can be used in RNA biosynthesis are:
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The bond between nucleotides in the primary structure of nucleic acid is...
The bond between nucleotides in the primary structure of nucleic acid is...
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The complementary pair of bases in the secondary structure of DNA is...
The complementary pair of bases in the secondary structure of DNA is...
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The secondary structure of DNA is stabilized by...
The secondary structure of DNA is stabilized by...
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Choose the tetrapeptide which has TWO amino acid residues with hydrophobic side chains:
Choose the tetrapeptide which has TWO amino acid residues with hydrophobic side chains:
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Choose the tetrapeptide which has THREE amino acid residues with hydrophilic side chains:
Choose the tetrapeptide which has THREE amino acid residues with hydrophilic side chains:
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Choose the tetrapeptide which has N-terminal amino acid residue with hydrophobic side chain:
Choose the tetrapeptide which has N-terminal amino acid residue with hydrophobic side chain:
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Choose the tetrapeptide which has TWO amino acid residues with hydrophilic side chains:
Choose the tetrapeptide which has TWO amino acid residues with hydrophilic side chains:
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Choose the tetrapeptide which has C-terminal amino acid residue with hydrophilic side chain:
Choose the tetrapeptide which has C-terminal amino acid residue with hydrophilic side chain:
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Choose the tetrapeptide which has THREE amino acid residues with hydrophilic side chains:
Choose the tetrapeptide which has THREE amino acid residues with hydrophilic side chains:
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The primary structure in ALL proteins is stabilized with…
The primary structure in ALL proteins is stabilized with…
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The secondary structure of proteins is stabilized ONLY with…
The secondary structure of proteins is stabilized ONLY with…
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The tertiary structure of proteins is stabilized with…
The tertiary structure of proteins is stabilized with…
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The quaternary structure of proteins is stabilized mainly with…
The quaternary structure of proteins is stabilized mainly with…
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Indicate a function which is NOT performed by proteins in humans:
Indicate a function which is NOT performed by proteins in humans:
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How is glucagon inactivated?
How is glucagon inactivated?
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Choose a pair of hormones regulating exchange of water and minerals.
Choose a pair of hormones regulating exchange of water and minerals.
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Choose a pair of hormones regulating reproductive functions.
Choose a pair of hormones regulating reproductive functions.
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Choose a pair of hormones regulating exchange of calcium and phosphates.
Choose a pair of hormones regulating exchange of calcium and phosphates.
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All effects listed below are shared by glucagon and cortisol except...
All effects listed below are shared by glucagon and cortisol except...
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Choose appropriate effects of cortisol.
Choose appropriate effects of cortisol.
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Choose appropriate effects of insulin action on cells.
Choose appropriate effects of insulin action on cells.
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Choose appropriate effects of adrenalin.
Choose appropriate effects of adrenalin.
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Choose appropriate effects of glucagon.
Choose appropriate effects of glucagon.
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Choose appropriate effects of insulin action on cells.
Choose appropriate effects of insulin action on cells.
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All metabolic pathways listed below do not work in erythrocytes except:
All metabolic pathways listed below do not work in erythrocytes except:
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Choose substance which decreases Hb affinity to oxygen.
Choose substance which decreases Hb affinity to oxygen.
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Choose a variant of Hb which cannot transport oxygen in blood.
Choose a variant of Hb which cannot transport oxygen in blood.
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ATP in red blood cells is used mainly for...
ATP in red blood cells is used mainly for...
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Increase of affinity and rate of O2 binding to Hb is a result of...
Increase of affinity and rate of O2 binding to Hb is a result of...
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Study Notes
Protein Structure, Properties, and Functions
- A protein's primary structure is stabilized by peptide bonds.
- The secondary structure of proteins is stabilized by hydrogen bonds.
- The tertiary structure of proteins is stabilized by covalent and noncovalent bonds.
- The quaternary structure of proteins is stabilized by noncovalent bonds and hydrophobic interactions.
- Functions of proteins in humans:
- Transport of hormones in blood
- Muscle contraction
- Storage of genetic information
- Catalysis of reactions
- Globulins are poorly dissolved in pure water, but their solubility can be increased by adding small amounts of NaCl.
- Protein-ligand interactions:
- Examples: antigen-antibody, hormone-receptor, and protein-heavy metal ion interactions
- Binding of ligand is highly specific and necessary for performing specific biological functions
Enzymes and Cofactors
- Cofactors:
- Vitamin B5 (nicotinic acid): part of coenzyme NAD
- Vitamin B2 (riboflavin): part of coenzyme FAD
- Vitamin B1 (thiamin): part of coenzyme TPP
- Vitamin B6: part of coenzyme pyridoxal phosphate
- Vitamin B9 (folic acid): part of coenzyme THF
- Enzyme cofactor functions:
- 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 classification:
- Transferases: catalyze the transfer of functional groups
- Ligases: catalyze the formation of covalent bonds
- Lyases: catalyze the cleavage of various chemical bonds
- Oxidoreductases: catalyze oxidation and reduction reactions
Energy Exchange
- Aerobic dehydrogenation: catalyzed by cytochrome oxidase
- Anaerobic dehydrogenation: catalyzed by succinate dehydrogenase
- Oxidation by removal of electrons: catalyzed by cytochrome a
- Dehydrogenation: a type of oxidation reaction in which electrons are removed from the substrate
- Monooxygenases: play a significant role in xenobiotics detoxication and the generation of reductive potentials
- Caloric coefficients:
- Carbohydrates: 4.1 kcal/g
- Proteins: 4.1 kcal/g
- Lipids: 9.3 kcal/g
- Daily requirements for food components (according to the WHO recommendations):
- Lipids: 1-2 g/kg body weight
- Proteins: 1-2 g/kg body weight
- Carbohydrates: 2-3 g/kg body weight
- Krebs cycle enzymes:
- Citrate synthase
- Aconitase
- Isocitrate dehydrogenase
- α-ketoglutarate dehydrogenase complex
- Succinyl-CoA-synthase
- Succinate dehydrogenase
- Fumarase
- Malate dehydrogenase
- Inhibitors of the respiratory chain:
- Complex I: rotenon
- Complex II: carboxin
- Complex III: antimycin
- Complex IV: carbon monoxide
- Uncoupling effect on oxidative phosphorylation:
- Caused by Dinitrophenol, Acetylsalicylic acid, and other substances
Carbohydrates
- Classification of carbohydrates:
- Monosaccharids: e.g., galactose
- Disaccharids: e.g., sucrose
- Homopolysaccharids: e.g., glycogen
- Heteropolysaccharids: e.g., hialuronic acid
- Metabolic pathways:
- Glycolysis: anaerobic oxidation of glucose
- Gluconeogenesis: synthesis of glucose from non-carbohydrate substances
- Pentose phosphate pathway: generation of NADPH+H+
- Glycogenesis: synthesis of glycogen from glucose
- Glucogenolysis: breakdown of glycogen to glucose### Carbohydrate Metabolism
- Digestion of glycogen and starch in the oral cavity is catalyzed by amylase.
- Digestion of disaccharides in the small intestine is catalyzed by sucrase, lactase, and maltase.
- All sugars can be absorbed in the intestinal wall, except lactose, ribose, and galactose.
- Products of food carbohydrates digestion in the GIT can be absorbed by active transport, facilitated diffusion, and simple diffusion.
- Hormones that have a hyperglycemic effect are glucagon, adrenalin, and cortisol, whereas insulin decreases blood glucose concentration.
- A patient has hyperglycemia if the concentration of glucose in blood is above 6.2 mmol/l, and hypoglycemia if it's below 3.6 mmol/l.
- Normal range of glucose concentration in blood in adults is 2.2-4.4 mmol/l.
- Physiologic hypoglycemia can be found in healthy persons in cases of starvation, and physiologic hyperglycemia in cases of overconsumption of food carbohydrates, long-term hard physical activity, or emotional stress.
Lipids
- Saturated fatty acids include palmitic acid, and polyunsaturated fatty acids include linoleic acid.
- Monounsaturated fatty acids include oleic acid.
- Eicosanoids are products of metabolism of the fatty acid arachidonic acid.
- The main function of triacylglycerols is energy storage.
- Cholesterol plays several physiological functions, including being a precursor for steroid hormones, and a component of cell membranes.
- The main function of eicosanoids is to act as regulative molecules of the paracrine system.
- Fatty acids may perform functions such as being structural components of cell membranes, and sources of energy.
- The main function of glycosphingolipids is to act as components of cellular membranes.
- The main function of glycerophospholipids is to act as components of cellular membranes.
- Ketone bodies can be synthesized in hepatocytes.
- Normal serum concentration range of ketone bodies is 0-30 mg/l.
Proteins and Amino Acids Exchange
- Essential amino acids include phenylalanine, methionine, tryptophan, and cysteine.
- Nitrogen equilibrium may be observed in healthy adults, and negative nitrogen balance may be observed in starvation state.
- Positive nitrogen balance may be observed in healthy children, and in cases of protein synthesis.
- Chymotrypsinogen is activated by trypsin.
- Amino acids can be used in protein synthesis, gluconeogenesis, and oxidative breakdown.
- Transamination is a process of transfer of an amino group from an amino acid to a keto acid.
- Transdeamination includes two reactions: transamination with oxaloacetate, and oxidative deamination of Asp.
- Enzymes that catalyze transdeamination reactions have cofactors such as pyridoxalphosphate and NAD+.
- Decarboxylation of amino acids and their metabolites needs a cofactor such as pyridoxalphosphate.
- The amino acid pool includes approximately 30 grams of free amino acids.
- Amino acids cannot be used in glycolysis.
- Choose the substance which is regenerated in each round of transdeamination reactions: α-ketoglutarate.
Nucleic Acids and Nucleotides
- The bases that can be found in purine nucleotides are adenine and guanine.
- The bases that can be found in pyrimidine nucleotides are thymin and cytosin.
- Monomers in the structure of RNA are AMP, GMP, CMP, and UMP.
- Monomers in the structure of DNA are dAMP, dGMP, dCMP, and dTMP.### DNA Biosynthesis
- Nucleotides used in DNA biosynthesis: dATP, dGTP, dCTP, dTTP
- Bond between nucleotides in primary structure of nucleic acid: 3',5'-phosphodiester bond
- Complementary pair of bases in secondary structure of DNA: Adenine-Thymine, Guanine-Cytosine
- Secondary structure of DNA is stabilized by: hydrogen bonds
DNA Folding
- Sequence of DNA folding events: Nucleosomes → 30-nm fibrils → Loops → Chromosomes
- Length of separate DNA molecule: several centimeters
- Enzyme that unwinds double helix during DNA replication: Helicase
- Enzyme that prevents supercoil formation during DNA replication: Topoisomerase
- Enzyme that synthesizes oligoribonucleotide during DNA replication: Primase
Regulation of Metabolism
- Hormone synthesis locations:
- Glucagon: Pancreatic gland
- Thyroxine: Thyroid gland
- Adrenalin: Medulla of suprarenal glands
- Somatotropin: Pituitary gland
- Hormone types:
- Peptide hormones: Glucagon, growth hormone, insulin
- Derivatives of amino acids: Adrenalin, thyroxine, T3, T4
- Steroid hormones: Aldosteron, cortisol, calcitriol, testosteron
- Hormone receptors:
- Insulin, growth hormone, glucagon: outer cell membrane
- Thyroxine, aldosteron: nucleus
- Adrenalin: outer cell membrane
- Hormone inactivation:
- Insulin: Oxidative deamination and conjugation
- Adrenalin: Oxidative deamination and methylation
- Glucagon: Proteolysis
Biochemistry of Blood, Liver, Kidney, and Connective Tissue
- Metabolic pathways in erythrocytes:
- Pentose phosphate pathway
- Anaerobic glycolysis
- Glutathione regeneration
- Substances that decrease Hb affinity to oxygen: 2,3-bisphosphoglycerate
- Variants of Hb: OxyHb, MetHb, HbF, CarboxyHb
- ATP usage in red blood cells: For active transport
- Pathologic variant of Hb: HbS
- Hyperazotemia: Urea nitrogen percentage more than 30%
- Glucokinase kinetic properties: High value of Km, not inhibited by glucose-6-phosphate
- Lipoproteins produced by hepatocytes: VLDL and HDL
- Bilirubin detoxication in the liver: Glucuronidation
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Prepare for your examination test with these questions on protein structure, properties, and functions. Identify tetrapeptides with hydrophobic and hydrophilic side chains.