- •Биологическая химия
- •060101 – Лечебное дело
- •Часть II
- •Contents
- •Cholesterol
- •I. Theoretical part
- •1. Lipids metabolism
- •1.1. Classification of lipids
- •2. Glycolipids (basically glycosphingolipids).
- •Galactosyl ceramide
- •1.2. Digestion and absorption of fats
- •Lipolysis of triglycerides in adipose tissue
- •1.3. Fatty acids oxidation
- •2. Transport of fa inside mitochondrion.
- •3 Ketocyl CoA tyolase Palmitic acid preformed rest Palmityl-CoA Acetyl-CoA
- •Oxidation of unsaturated fatty acids
- •Violations of fatty acids oxidation
- •Acetyl-CoA metabolism
- •1.4. Lipogenesis
- •Regulation of fatty acids synthesis and break down
- •1.5. Metabolism of phospholipids
- •1.6. Essencial fatty acids. Eicosanoids
- •1.7. Cholesterol metabolism
- •Distribution and functions of cholesterol
- •Cholesterol biosynthesis
- •1. Conversion of active acetate into mevalonic acid.
- •2. Squalene formation from mevalonic acid.
- •Regulation of cholesterol synthesis
- •Cholesterol esters metabolism
- •Synthesis of bile acids
- •1.8. Regulation of lipid metabolism
- •1.9. Violations of lipid metabolism
- •Violation of fats adsorption processes:
- •Test questions
- •2. Proteins metabolism
- •2.1. Pathways of proteins degradation
- •2. Digestion of proteins.
- •The selectivity of peptidases
- •2.2. Amino acids metabolism
- •The reactions of amino groups
- •Intramolecular deamination.
- •Reactions of the carboxyl group
- •2. Aminoacyladenylate formation.
- •2.3. Ammonia neutralization in the body
- •Storage and transport of ammonia
- •Fumarate pyruvate aspartate
- •2.4. Violations of nitrogen metabolism
- •2.5. Metabolism of individual amino acids
- •2. Metabolism of sulfur amino acids.
- •3. Metabolism of branched chain amino acids.
- •Leu, Ile, Val α-keto acids acyl-CoA derivatives
- •4. Metabolism of dicarboxylic amino acids
- •5. Metabolism of diaminomonocarboxylic acids.
- •6. Metabolism of phenylalanine and tyrosine.
- •7. Metabolism of tryptophan.
- •2.6. Metabolism of conjugated proteins. Chromoproteins metabolism
- •The degradation of hemoglobin in the tissues (the formation of bile pigments)
- •The hemoglobin biosynthesis
- •2.7. Nucleoproteins metabolism
- •Adenine hypoxanthine; guanine xanthine
- •The synthesis of pyrimidine nucleotides u, c, t
- •I nosine-5'-phosphate Xantosine-5'-phosphate
- •The synthesis of deoxyribonucleotides
- •Test questions
- •3. Template biosynthesis
- •3.1. Biosynthesis of nucleic acids
- •3.1.1. Dna biosynthesis (replication)
- •Synthesis of dna in the rna template
- •3.1.2. Rna biosynthesis
- •Rna synthesis in rna template
- •3.2. Protein biosynthesis
- •The properties of the genetic code
- •Preparatory stage of protein synthesis
- •3.2.1. Translation
- •1. Initiation.
- •2. Elongation.
- •3.2.2. Post-translational modification of proteins
- •Transport of synthesized proteins through membranes
- •3.2.3. Regulation of protein biosynthesis
- •3.3. Genetic engineering
- •Test questions
- •4. Hormones, nomenclature, classification
- •Test questions
- •5. Metabolic processes interaction
- •In the organism
- •Protein and carbohydrate metabolisms interconnection
- •Protein and lipid metabolisms interconnection
- •Carbohydrate and lipid metabolisms interconnection
- •Levels of homeostasis regulation
- •Changes in metabolism during starvation
- •Test questions
- •6. Mineral and water and salt metabolism
- •6.1. Water in the human body
- •6.2. Salt metabolism
- •7. Renal biochemistry. The role of the kidneys in the regulation of water and salt metabolism
- •7.1. Excretory function of the kidneys
- •7.2. Homeostatic function of the kidneys
- •7.3. Metabolic functions of the kidneys
- •7.4. Regulation of water and salt metabolism and uropoiesis
- •Test Questions
- •8. Biochemistry of nervous tissue
- •8.1. Features of metabolism of nervous tissue
- •8.2. Mechanism of nerve impulses conduction
- •Cholinergic synapses
- •Test Questions
- •9. Biochemistry of muscle tissue
- •9.1. Chemical composition of muscle tissue
- •Sources of energy for muscle work
- •9.2. Mechanism of muscle contraction and its regulation
- •9.3. Biochemical changes in muscles within pathology
- •Test Questions
- •10. Biochemistry of extracellular matrix
- •10.1. Structure of extracellular matrix
- •Collagens.
- •Fibril-forming collagens
- •Collagen, forming a tela
- •10.2. Features of metabolism of extracellular matrix Catabolism of extracellular matrix proteins
- •Reparation of damage of the extracellular matrix in norm
- •Biochemical changes of connective tissue with aging
- •The lesions of connective tissue
- •11. Blood biochemistry
- •11.1. Respiratory function of blood. Buffer systems of blood
- •11.2. Blood coagulation system. Changes in pathology
- •Extrinsic and intrinsic pathways of blood clotting
- •Test Questions
- •12. Liver biochemistry
- •12.1. Main functions of the liver
- •The role of the liver in the metabolism of carbohydrates
- •The role of liver in lipid metabolism
- •The role of the liver in the metabolism of proteins and amino acids
- •12.2. Choleresis. Pigment metabolism. Types of jaundice
- •The cleavage of hemoglobin: hemoglobinverdoglobinbiliverdinbilirubin.
- •12.3. Detoxifying liver function
- •Test Questions
- •13. Regulation of calcium and phosphorus metabolism
- •14. Bone biochemistry
- •Test Questions
- •II. Laboratory workshop Laboratory work 1. Lipid metabolism
- •Hydrolysis of milk fat by lipase
- •Test Questions
- •Laboratory work 2. Phospholipids. Cholesterol
- •4.1. Schiff reaction.
- •4.2. Salkowski reaction.
- •4.3. Lieberman-Burchard reaction.
- •Preparation of solutions of cholesterol for the calibration curve
- •Test Questions
- •Laboratory work 3. Digestion of proteins. Determination of acids of gastric contents
- •Experiment 2. Qualitative determination of free hydrochloric acid in gastric juice using indicator congo red.
- •Results of the determination of gastric acidity
- •Test Questions
- •Laboratory work 4. The end products of nitrogen metabolism
- •Test Questions
- •Laboratory work 5. Hormones
- •2.1. Biuretic reaction.
- •2.2. Millon’s reaction.
- •2.4. Geller’s test.
- •3. Qualitative reaction to thyroxine.
- •4. Qualitative reactions to the 11-dehydro-17-oxykortikosteron (cortisone).
- •4.1. The reaction with phenylhydrazine sulfate.
- •4.2. The reaction with Fehling's reagent.
- •Test Questions
- •Laboratory work 6. Mineral and water and salt metabolism
- •1.1. Determination the pH of saliva.
- •1.2. Detection of phosphates in saliva.
- •2.1. Qualitative detection of chlorides in the urine.
- •2.2. Detection of calcium in the urine.
- •2.3. Detection of phosphates in the urine.
- •The composition of mixtures for the calibration curve
- •Test Questions
- •Laboratory work 7. Urine biochemistry
- •3.1. Qualitative detection and quantitative determination of protein in the urine.
- •3.1.1. The test by boiling in weak acid environment.
- •3.1.2. The test by boiling in an acid medium in the presence of saturated sodium chloride solution.
- •3.1.3. Geller’s test.
- •3.1.4. The test with sulfosalicylic acid.
- •3.1.5. Quantitative determination of protein in the urine by the method of dilution (Brandberg - Roberts - Stolnikov method).
- •Determination of protein in the urine using dilution method
- •3.2. Semi-quantitative method for determining glucose and ketone bodies in urine using test strips.
- •3.3. Detection of blood pigments in the urine by boiling with alkali (Geller’s test).
- •Test Questions
- •Laboratory 8. Blood biochemistry
- •1. Buffer properties of blood serum.
- •2. Quantitative determination of total protein in serum according to biuretic reaction.
- •The composition of mixtures for the ployying of the calibration curve
- •3. Determination of calcium in serum by the method of de Waard.
- •Test Questions
- •Laboratory work 9. Detection of bile pigments in urine
- •Test Questions
- •Laboratory work 10. Biochemistry of bone and connective tissue
- •1. Preparation of extracts of bone and teeth tissues.
- •Test Questions
- •Bibliography
- •Biochemistry
- •In Two Parts Part II
- •392008, Г. Тамбов, ул. Советская, 190г
Rna synthesis in rna template
Viral RNA induces the formation of RNA-dependent RNA polymerase in host cells, which is involved in the replication of viral RNA. Examples are viruses of influenza, rabies, mumps, and measles. RNA replicase constructs complementary RNA strand on the template virus RNA. It serves as a template for RNA synthesis, the same type of initial viral RNA. Both stages are catalyzed by the same enzyme, although each involves different protein factors.
Since the RNA replicase is related only to the virus, obviously, effective antiviral drugs can be developed on this basis.
3.2. Protein biosynthesis
Protein synthesis is closely connected to the concept of genetic code.
Genetic code is the way to codify amino acid sequence with the help of sequence of nucleotides in all living organisms.
The properties of the genetic code
1. Triple character. The unit of code is a combination of three nucleotides (triplet or codon). All in all there are 64 codons, in other words, each amino acid is codified by three nucleotides in mRNA.
2. Continuity. There are no commas or punctuation signs between the triplets, that is, information is read continuously.
3. Non-overlapping. One and the same nucleotide could not be simultaneously in the structure of two or more triplets.
4. Specificity. A particular codon codes for only one amino acid (AUU is isoleucine, UUU is phenylalanine).
5. Degenerate. One amino acid could correlate to several codons (isoleucine is AUU, AUC, AUA).
6. Universality. Genetic code work is the same in the organism of different structures from viruses to humans.
Preparatory stage of protein synthesis
20 amino acids, 20 aminoacyl-tRNA-synthetases, more than 20 tRNA, ATP, magnesium ions are necessary.
Amino acid reacts with ATP with the formation of aminoacyl-adenylate, then amino acid is transported from aminoacyladenylate to acceptor stem of tRNA (3’-end):
R–CH(NH2)–COOH + АТP R–CH(NH2)–COO–АМP + PPi
aminoacyladenylate
R–CH(NH2)–COO–АМP + tRNA
R–CH(NH2)–COO–tRNA+ АМP
An enzyme here is aminoacyl-tRNA-synthetase. The presence of magnesium ions is necessary. Aminoacyl-tRNA-synthetases are characterised by absolute specificity. Each amino acid has its own enzyme.
Transfer RNA (tRNA) provides connection between codons of mRNA and amino acids of the future polypeptide chain. There is not less than one tRNA for each amino acid out of 20 amino acids. Each tRNA has about 80 nucleotides. They have the structure of clover leaf in 2-dimensional shape and L-structure in the 3-dimensional shape (Fig. 3).
Fig. 3. The structure of tRNA
The acceptor stem is the site for amino acids binding. It contains CCA sequence.
The TC (pseudouridilic) loop provides aminoacyl-tRNA binding with ribosome.
The D (dihydrouridilic) loop is a site for the recognition of aminoacyl-tRNA synthetase.
Anticodon loop contains an anticodon which is complimentary to the codon in the mRNA It has 3 nucleotide residues.
A destination of the variable loop is unknown.
