“Metabolism and cell energy” - Definition. Plastic exchange. Digestive organs. Preparing students for open-ended tasks. Chemical transformations. Questions with “yes” or “no” answers. Metabolism. Metabolism. Text with errors. A task with a detailed answer. Test tasks. Energy exchange.
“Metabolism” - Properties of the genetic code. Molecular weight of one amino acid. Genetic code. The initial part of the molecule. Plastic exchange. Transcription. Protein. DNA. Determine the length of the corresponding gene. Reactions of assimilation and dissimilation. A section of the right strand of DNA. Define the terms. Autotrophs. Protein biosynthesis. What primary structure will the protein have? A protein consisting of 500 monomers. Broadcast.
“Energy metabolism” 9th grade - Glucose is the central molecule of cellular respiration. ATP in numbers. The concept of energy metabolism. Autotrophs. PVA – pyruvic acid C3H4O3. Structure of ATP. ATP is a universal source of energy in the cell. Conversion of ATP to ADP. Fermentation is anaerobic respiration. Metabolism. Energy metabolism in the cell. Fermentation. Energy metabolism (dissimilation). Mitochondria. The aerobic stage is oxygen. Summary equation of the aerobic phase.
“Stages of Energy Metabolism” - Summary Equation. Types of nutrition of organisms. The splitting process. Metabolism. Oxidation of PVC. Electron transport chain. Energy release. Krebs cycle. Describe the reactions. Oxidative decarboxylation. Catabolism. Aerobic respiration. Stages of aerobic respiration. Preparatory stage. Oxygen splitting. Solar energy. Where does ATP synthesis take place? Oxygen-free stage. Fill in the blanks in the text.
“Carbohydrate metabolism” - Summary of the Krebs cycle. Triosephosphate isomerase. Sucrose. Chemiosmotic model of ATP synthesis. Factors influencing enzyme activity. Metabolism. Glycolysis. Aldolase. Classification of enzymes. Stocking. Stages of glucose oxidation. Formation of branches. Enzymes. Protein components of the mitochondrial ETC. Enzymes. The main stages of carbohydrate metabolism. Enolase. Glycogen synthesis. Oxidation of acetyl-CoA to CO2.
“Energy metabolism” - The process of energy metabolism. Glycolysis. Energy released in glycolysis reactions. Enzymes of the oxygen-free stage of energy exchange. The fate of the PVK. Lactic acid fermentation. Lactic acid. Biological oxidation and combustion. Oxidation of substance A. Preparatory stage. Repetition. Combustion. Energy exchange.
Squirrels- high molecular weight natural polymers consisting of amino acid residues , connected by a peptide bond; are the main component of living organisms and the molecular basis of life processes.
More than 300 different amino acids are known in nature, but only 20 of them are part of the proteins of humans, animals and other higher organisms. Each amino acid has carboxyl group, amino group in the α-position (at the 2nd carbon atom) and radical (side chain), which differs among different amino acids. At physiological pH (~7.4), the carboxyl group of amino acids usually dissociates and the amino group is protonated.
All amino acids (with the exception of glycine) contain an asymmetric carbon atom (i.e., such an atom, all four valence bonds of which are occupied by different substituents, it is called a chiral center), therefore they can exist in the form of L- and D-stereoisomers (the standard is glyceraldehyde ):
For the synthesis of human proteins, only L-amino acids are used. In proteins with a long lifespan, L-isomers can slowly acquire the D-configuration, and this happens at a certain rate characteristic of each amino acid. Thus, dentin proteins of teeth contain L-aspartate, which transforms into the D-form at human body temperature at a rate of 0.01% per year. Since dental dentin is practically not exchanged or synthesized in adults in the absence of trauma, the D-aspartate content can be used to determine a person’s age, which is used in clinical and forensic practice.
All 20 amino acids in the human body differ in structure, size and physicochemical properties of the radicals attached to the α-carbon atom.
The structural formulas of 20 proteinogenic amino acids are usually given in the form of the so-called proteinogenic amino acid tables:
Recently, single-letter designations have been used to designate amino acids; a mnemonic rule (fourth column) is used to remember them.
CH 3 CH 3
IET is in the region of pH≈7
GLI - GLU
(CH 2) 2 -COOH (CH 2) 2 - COOH
IET is in the pH region<7
GLI - LIZ
H 2 N–CH 2 –CO–NH–CH–COOH ↔ H 3 N + –CH 2 –CO–NH–CH–COO ‾
(CH 2) 4 –NH 2 (CH 2) 4 – NH 2
IET is in the pH>7 region
16.4 PROTEINS
Proteins are high-molecular nitrogen-containing biological macromolecules consisting of biogenic α,L-amino acids linked in a linear sequence by peptide (amide) bonds.
The simplest protein is a polypeptide containing at least 70 amino acid residues in its structure.
Proteins are the most important components of the cell, accounting for at least 50% of dry weight. They carry out the implementation of genetic information, the construction of cell and body structures, the occurrence of metabolic processes, and the body’s immune defense.
The difference between peptides and proteins is not only quantitative, but also qualitative. After the biosynthesis of the polypeptide chain of proteins on ribosomes and its subsequent convergence into the hydrophilic environment of the cytosol, higher levels of its organization spontaneously form - secondary, tertiary, and for a number of proteins - quaternary structure.
1. Primary structure– is defined as a linear sequence of biogenic amino acids linked by peptide bonds. It is genetically determined for each specific protein in the nucleotide sequence of messenger RNA. The primary structure also determines higher levels of organization of protein molecules. Knowing the primary structure, it is possible to consistently obtain a protein synthetically (insulin was synthesized for the first time, and subsequently many other proteins, so synthetic polypeptides became widespread for the treatment of AIDS and many other diseases).
2. Secondary structure protein - a local conformation of a polypeptide chain, resulting from the rotation of its individual sections, leading to twisting, folding or bending of this section of the chain. The secondary structure can be represented by an α-helix, β-structure (structure
folded sheet).
3. Tertiary structure- conformation (location in space) of the entire polypeptide chain, determined by the interaction of elements of the secondary structure of both nearby and distant amino acid residues. All types of interactions take part in its formation and stabilization: hydrophobic, van der Wals, electrostatic (ionic), disulfide covalent bonds. The most significant are hydrophobic interactions and disulfide bonds.
4. Quaternary structure squirrel. A method of spatial arrangement of individual polypeptide chains (identical or different) with a tertiary structure, leading to the formation of a structurally and functionally unified macromolecular formation ( multimer).
Each individual polypeptide chain in the multimer structure is called protomer. The protomers are sterically complementary and bind the structure together through noncovalent bonds. For example, the protein molecule that makes up the blood, hemoglobin, consists of several symmetrically constructed particles (identical polypeptide chains) that have the same primary, secondary and tertiary structure.
Anna Provisorova
phone/viber: +79209794102
higher education
part-time study
"Peptide Synthesis"
(position) (full name)
Tomsk-201__
Dear students!
You have studied the section “Nucleic acids. Matrix biosyntheses" distance course "Biological chemistry"
On the topic "Peptide Synthesis"
Select a peptide from the list,
in this case, the peptide number must correspond to your serial number in the end-to-end alphabetical list of course students
PEPTIDE OPTIONS
|
1. val-glu-cis |
2. val-asp-cis |
3. val-ala-cis |
4. val-tir-cis |
5. val-phencis |
|
6. gly-glu-three |
7. gli-asp - three |
8. gli-ala - three |
9. glitir - three |
10. glyphen - three |
|
11. ala-glu-gln |
12. ala-asp - gln |
13. ala-val - gln |
14. alatir - gln |
15. ala-fen - gln |
|
16. lei-glu-tir |
17. lei-asp-tyr |
18. lei-ala-tir |
19. leu-thyr-cis |
20. lei-fen-tir |
|
21. ili-glu-asp |
22. ili-asp-lys |
23. ilei-ala - asp |
24. iley-tir - asp |
25. ilei-fen-asp |
|
26. ser-glu-met |
27. ser-asp - met |
28. serala - met |
29. ser-tir - meth |
30. serfen - meth |
|
31. tr-glu-cis |
32. tre-asp - cis |
33. treal - cis |
34. ter- ter cis |
35. trefen - cis |
|
36. cis-glu-pro |
37. cis-asp - about |
38. cis-ala - about |
39. cis-tir - about |
40. cis-phene - about |
|
41. met-glu-yl |
42. met-asp-iley |
43. metal - silt |
44. met-tir - ili |
45. met-phen-yl |
|
46. fen-gluley |
47. fen-asp - lei |
48. fen-ala - lei |
49. fen-tir - lei |
50. fen-fen - lei |
|
51. tir-glu-gis |
52. thyr-asp-gis |
53. tir-ala - gis |
54. tir-tir - gis |
55. tir-fen - gis |
|
56. three-glu-arg |
57. tri-asp - arg |
58. trial-ala - arg |
59. tri- tier - arg |
60. triphen - arg |
|
61. asn-glu-lyse |
62. ala-asp-liz |
63. ala-ala - liz |
64. alatir - liz |
65. ala-fen - lys |
|
66. about-glu-three |
67. pro-asp - three |
68. pro-ala - three |
69. wipe - three |
70. profen - three |
|
71. lys-glutyre |
72. lis-asp - shooting range |
73. licked - shooting range |
74. lys- tyr - ser |
75. liz-fen - shooting range |
|
76. arg-glu-fen |
77. arg-asp - hairdryer |
78. argala - hairdryer |
79. arg-tir - hairdryer |
80. arg-fen - ala |
|
81. gis-glu-tre |
82. gis-asp - tre |
83. gisala - tre |
84. histir - tre |
85. hysphene - tre |
|
86. val-glu-ser |
87. val- asp - gray |
88. val-ala - gray |
89. val-tir - ser |
90. val-fen - ser |
|
91. ala-glu-cis |
92. ala-asp-cis |
93. ala-ala - cis |
94. alatir - cis |
95. ala-fen - cis |
|
96. fen-asp-gli |
97. fen-asp - gli |
98. fen-ala - gly |
99. fen-tir - gli |
100. fen-fen-gli |
|
101. val-lys-cis |
102. val-gis-cis |
103. val-arg-cis |
104. val-leu-cis |
105. val-pro-cis |
|
106. glilyz - three |
107. gligis - three |
108. gli-arg - three |
109. gli-ley - three |
110. glilyz - three |
|
111. alaliz - gln |
112. alagis - gln |
113. ala-arg - gln |
114. ala-ley - gln |
115. ala-arg - gln |
|
116. ley-liz-tir |
117. lei-gis-tyr |
118. lei-arg-tir |
119. lei-ley-cis |
120. lei-gis-tyr |
|
121. iley-lys - asp |
122. ileigis - asp |
123. ili-arg - asp |
124. ili-ley - asp |
125. ili-gli-asp |
|
126. Serlys - meth |
127. sergis - met |
128. ser-arg - met |
129. surley - meth |
130. serala - met |
|
131. trelize - cis |
132. tregis - cis |
133. tr-arg - cis |
134. trill cis |
135. treval - cis |
|
136. cis-lys - about |
137. cis-gis - about |
138. cis-arg - about |
139. cis-le - about |
140. cis-le - about |
|
141. metalliz - ili |
142. met-gis - ili |
143. met-arg - ili |
144. broom - mud |
145. meth-ile-pro |
|
146. fen-liz - lei |
147. fengis - lei |
148. fen-arg - lei |
149. fen-ley - lei |
150. fen-ser - lei |
|
151. tir-liz - gis |
152. tir-gis-ala |
153. tir-arg-gis |
154. tyr-ley - gis |
155. tir-tre - gis |
|
156. triliz - arg |
157. trigis - arg |
158. tri-arg - arg |
159. tri-t lei - arg |
160. tricis - arg |
|
161. asn-liz - val |
162. alagis - liz |
163. ala-arg-liz |
164. ala-ley - liz |
165. ala-met - liz |
|
166. proliz - three |
167. progis - three |
168. pro-arg - three |
169. spill - three |
170. profen - three |
|
171. liz-liz - shooting range |
172. lys-gis - shooting range |
173. lis-arg - shooting range |
174. lisley - gray |
175. lys- tyr - tyr |
|
176. argliz - hairdryer |
177. arg-gis - hairdryer |
178. arg-arg - hairdryer |
179. argley - hairdryer |
180. arg-tri - ala |
|
181. gis-liz - tre |
182. gis-gis - tre |
183. gis-arg - tre |
184. gis-lei - tre |
185. gis-asp - tre |
|
186. Wallis - gray |
187. valgis - ser |
188. val-arg - ser |
189. valley - ser |
190. val-glu-ser |
|
191. alaliz - cis |
192. alagis - cis |
193. ala-arg - cis |
194. ala-ley - cis |
195. ala-asn-cis |
|
196. fen-lyz - gli |
197. fengis - gly |
198. fen-arg-gli |
199. fen-ley - gly |
200. fen-gln-gly |
1. Write the nucleotide composition of the gene encoding the synthesis of the peptide.
2. Write the composition of the tRNA anticodon loop.
3. Write the activation reactions of amino acids.
4. Describe the stages of peptide synthesis on ribosomes.
5. In the structure of DNA and RNA required for peptide synthesis, indicate the number of purine and pyrimidine nucleotides.
6. What products are formed during the breakdown of these purines and pyrimidines. nucleotides that make up the DNA encoding this peptide.
Answers:
Federal State Budgetary Educational Institution
higher professional education
"Siberian State Medical University"
Ministry of Health of the Russian Federation
(Federal State Budgetary Educational Institution of Higher Education Siberian State Medical University of the Ministry of Health of Russia)
Individual task
part-time study
"Hormones"
Completed by: ________________ /___________/
(position) (full name)
Tomsk-201_
Dear students!
You have studied the section “Hormones. Biochemistry of Organs and Tissues" distance course "Biological Chemistry"
Hormones»
Exercise 1
Patient N. received prednisolone for a long time for the treatment of infectious polyarthritis. Having felt an improvement, the patient voluntarily stopped taking the drug. Soon the patient's condition deteriorated sharply. During the examination, he was found to have a decrease in blood glucose concentration and a decrease in blood pressure. The content of 17-ketosteroids in urine decreased. Why did the patient's condition worsen? To answer:
1. Describe the mechanism of regulation of the synthesis and secretion of the hormone, the production of which was suppressed in the patient as a result of long-term use of prednisolone.
2. Name the reasons for the decrease in the concentration of glucose in the blood and 17-ketosteroids, and the decrease in blood pressure.
Answers:
Task 2
A 43-year-old patient consulted a doctor with a complaint of sudden attacks, accompanied by severe weakness, headache, hunger, often numbness in various parts of the body, stiffness in movements and, at the same time, an excited state. Attacks occur on an empty stomach or 2-3 hours after eating, when performing physical activity. After eating, the attack goes away. The concentration of C-peptide in the blood is increased. What disease are these symptoms characteristic of? To answer:
1. Indicate what biochemical studies, in addition to determining the concentration of C-peptide, must be performed to establish a diagnosis.
2. Suggest the diagnosis that was made by the doctor and explain the molecular mechanisms behind the development of its symptoms.
Answers:
Task 3
A 60-year-old woman consulted a doctor with complaints of fatigue, chilliness, drowsiness, memory loss, and weight gain. The examination revealed moderate obesity, dry, cold skin and a puffy face. The thyroid gland is not palpable. A blood test showed: thyroxine - 15 nmol/l, TSH - 25 mU/l. Explain the reasons for changes in the level of these hormones in the patient’s blood. To answer:
1. Describe the stages of iodothyronine synthesis.
2. How the synthesis and secretion of iodothyronines is regulated, indicate the pathways for transmitting the hormonal signal to target cells.
3. List the target tissues and the main physiological effects of thyroxine.
Answers:
9//Federal state budgetary educational institution
higher education
"Siberian State Medical University"
Ministry of Health of the Russian Federation
(Federal State Budgetary Educational Institution of Higher Education Siberian State Medical University of the Ministry of Health of Russia)
Individual task
for 3rd year students of the Faculty of Pharmacy,
part-time study
"The role of P-glycoprotein in the development of drug resistance"
Completed by: ________________ /___________/
(position) (full name)
Tomsk-201_
Dear students!
You have studied the “Pharmaceutical Biochemistry” section of the distance learning course
"Biological chemistry"
To consolidate theoretical knowledge and master practical skills, it is necessary to complete an individual task
on this topic " The role of P-glycoprotein in the development of drug resistance»
P-glycoprotein is an ATP-dependent transmembrane transporter and transports various cytotoxic substances from the cell, i.e. their efflux into the intestinal lumen, reducing their absorption. Most drugs (glucocorticoids, anticancer drugs, macrolides, statins) are P-glycoprotein substrates. The degree of effectiveness of these substances depends on the full functioning of P-glycoprotein. The search for selective P-glycoprotein inhibitors is the basis of individualized pharmacotherapy.
Complete an individual task according to the following plan:
1. The structure of P-glycoprotein.
2. Localization in cells.
3. Gene polymorphism.
4. Substrates, inhibitors and inducers of P-glycoprotein.
5. The role of P-glycoprotein in primary and secondary multidrug resistance.
6. Provide a list of references used.
Answers:
Federal State Budgetary Educational Institution
higher education
"Siberian State Medical University"
Ministry of Health of the Russian Federation
(Federal State Budgetary Educational Institution of Higher Education Siberian State Medical University of the Ministry of Health of Russia)
Individual assignment for students
3 years of Faculty of Pharmacy,
part-time study
"Protein catabolism"
Completed by: ________________ /___________/
(position) (full name)
Tomsk-201__
Dear students!
You have studied the “Protein Metabolism” section of the distance learning course “Biological Chemistry”
To consolidate theoretical knowledge and master practical skills, it is necessary to complete an individual assignment on the topic “Protein Catabolism”
Select a topic from the list,
1. Chicken egg protein catabolism
2. Meat protein catabolism
3. Milk protein catabolism
4. Soy protein catabolism
5. Bean protein catabolism
6. Catabolism of sturgeon caviar proteins
7. Catabolism of red fish proteins
8. Catabolism of seafood proteins (shrimp)
9. Catabolism of rabbit meat proteins
10. Cheese protein catabolism
Prepare your answer according to the following plan:
1. Characterize the amino acids that make up the protein according to their biological functions.
2. What is the IET of this protein and what does it mean.
3. Suggest a method by which protein concentration can be determined. State the principle of the method.
4. List and characterize the specificity of gastrointestinal enzymes capable of hydrolyzing this protein. Specify hydrolysis products.
5. Describe the mechanism of absorption and metabolic pathways of amino acids obtained from protein hydrolysis.
6. List the ways in which these amino acids are used in the body.
7. Write the deamination reaction of one of the amino acids that make up the protein. What enzymes and vitamins are required for these processes?
8. Write the reaction of decarboxylation of one of the amino acids that make up the protein, as a result of which biogenic amines are formed. What enzymes and vitamins are required for these processes?
9. What toxic products can be formed with an excess of this protein?
10. Write two reactions for the neutralization of ammonia.
Federal State Budgetary Educational Institution
higher education
"Siberian State Medical University"
Ministry of Health of the Russian Federation
(Federal State Budgetary Educational Institution of Higher Education Siberian State Medical University of the Ministry of Health of Russia)
Individual task
for 3rd year students of the Faculty of Pharmacy,
part-time study
"Energetic effect of carbohydrate oxidation"
Completed by: ________________ /___________/
(position) (full name)
Tomsk-201__
Dear students!
To consolidate theoretical knowledge and master practical skills, it is necessary to complete an individual task
on this topic " Energy effect of carbohydrate oxidation»
Select a topic from the list,
in this case, the topic number must correspond to the last digit of the grade book number
1. Energy effect of anaerobic glucose oxidation
2. Energy effect of complete oxidation of glucose-1-phosphate
3. Energy effect of fructose oxidation
4. Energy effect of glyceroaldehyde phosphate oxidation
5. Energy effect of dihydroxyacetone phosphate oxidation
6. Energy effect of fructose-1,6-bisphosphate oxidation
7. Energy effect of galactose oxidation
8. Energy effect of maltose oxidation
9. Energy effect of sucrose oxidation
10. Energy effect of lactose oxidation
Prepare your answer according to the following plan:
1. The source and stages of formation of this substance from carbohydrates supplied with food, indicating the enzymes of the gastrointestinal tract.
2. Ways to use this substance in the body.
3. Describe the stages of metabolism associated with the formation of NADH, FADH2, ATP, GTP, ATP.
4. If NADH is formed in the cytoplasm, then indicate the mechanism of transport to the mitochondria to the respiratory chain, where ATP will be synthesized.
5. Indicate the method of ATP synthesis (phosphorylation): substrate or oxidative.
6. Compare the resulting energy yield with the amount of ATP formed during the complete oxidation of glucose.
Answers:
Federal State Budgetary Educational Institution
higher education
"Siberian State Medical University"
Ministry of Health of the Russian Federation
(Federal State Budgetary Educational Institution of Higher Education Siberian State Medical University of the Ministry of Health of Russia)
Individual task
for 3rd year students of the Faculty of Pharmacy,
part-time study
"Faty acid metabolism"
Completed by: ________________ /___________/
(position) (full name)
Tomsk-201_
Dear students!
You have studied the “Carbohydrates” section of the distance learning course “Biological Chemistry”
To consolidate theoretical knowledge and master practical skills, it is necessary to complete an individual task
on this topic " Fatty acid metabolism»
Select a topic from the list, in this case, the topic number must correspond to the last digit of the grade book number
1. Decomposition and synthesis of myristic acid
2. Decomposition and synthesis of palmitic acid
3. Decomposition and synthesis of stearic acid
4. Decomposition and synthesis of arachidic acid
5. Decomposition and synthesis of lignoceric acid
6. Decomposition and synthesis of oleic acid
7. Decomposition and synthesis of nervonic acid
8. Decomposition and synthesis of lenoleic acid
9. Linolenic acid metabolism
10. Arachidonic acid metabolism
Prepare your answer according to the following plan:
1. Indicate the products that contain this acid.
2. Write the stages of fat digestion in the gastrointestinal tract, indicating the role of bile acids, enzymes and the mechanism of absorption.
3. List the catabolic and anabolic pathways of fatty acid use.
4. Calculate the number of ATP molecules that are formed during b-oxidation of fatty acid.
5. Indicate the ways of using acetyl-CoA formed during the breakdown of fatty acids.
6. Write the stages of synthesis of this fatty acid in the body.
7. Draw up a scheme for the synthesis of this acid from the products of glucose metabolism.
Answers:
Federal State Budgetary Educational Institution
higher education
"Siberian State Medical University"
You have studied the section “Biological oxidation. Respiratory chain" distance course "Biological chemistry"
To consolidate theoretical knowledge and master practical skills, it is necessary to complete an individual assignment on the topic “ Respiratory chain»
Select a substrate from the list, in this case, the topic number must correspond to the last digit of the grade book number
1. a-Ketoglutarate (last digit 1.6)
2. Isocitrate (last digit 2.7)
3. Pyruvate (last digit 3, 8)
4. Malat (last digit 4.9)
5. Succinate (last digit 5.10)
Prepare your answer according to the following plan:
1. Name the enzyme that catalyzes the oxidation of the substrate.
2. Name the coenzyme (reduced equivalent).
3. To which part of the respiratory chain will the reduced equivalent of electrons and protons be transferred?
Anna Pharmacist / taurusann
Dear Colleagues! Since studying becomes more and more difficult every year, I offer my services in solving various pharmaceutical disciplines. Sometimes, even if you study well, you cannot do everything, so contacting me in a timely manner will help prevent and solve many problems for you.
differs from the similar polypeptide in bovine TSH
amino acid residues and the absence of C-terminal methionine. By-
the properties of the hormone are explained by the presence of the β-subunit of TSH in the complex
with the α subunit. It is assumed that the action of thyrotropin is carried out
occurs, like the action of other hormones of protein nature, through
binding to specific receptors of plasma membranes and ac-
titration of the adenylate cyclase system (see below).
Gonadotropic hormones (gonadotropins)
Gonadotropins include follicle-stimulating hormone (FSH,
follitropin) and luteinizing hormone (LH, lutropin), or hormone,
stimulating interstitial cells *. Both hormones are synthesized
in the anterior lobe of the pituitary gland and, like thyrotropin, are complex
proteins - glycoproteins with mol. weighing 25,000. They regulate the ste-
Roido- and gametogenesis in the gonads. Follitropin causes maturation
formation of follicles in the ovaries in females and spermatogenesis in males. Lutropin
in females it stimulates the secretion of estrogen and progesterone, as well as rupture
follicles with the formation of the corpus luteum, and in males - the secretion of dough-
sterone and interstitial tissue development. Biosynthesis of gonadotropins,
as noted, is regulated by the hypothalamic hormone gonadolibo-
The chemical structure of the lutropin molecule has been completely deciphered.
Lutropin consists of two α- and β-subunits. Structure of α-subunits
hormone is the same in most animals. So, in a sheep it contains 96
amino acid residues and 2 carbohydrate radicals. In humans, the α-subunit
The hormone chain is shortened by 7 amino acid residues from the N-terminus and differs
It is the nature of 22 amino acids. The sequence has also been deciphered
amino acids in the β-subunits of pig and human lutropin. α- and β-Sub-
units individually lack biological activity (by analogy
with most enzyme subunits). Only their complex, education
which, most likely, is predetermined by their primary structure,
leads to the formation of a biologically active macromolecular structure
tours due to hydrophobic interactions.
Lipotropic hormones (LTH, lipotropins)
Among the hormones of the anterior pituitary gland, the structure and function of which
clarified in the last decade, it should be noted lipotropins, in particular
ity of β- and γ-LTG. The primary structure of β-lipo-
sheep and pig tropina, whose molecules consist of 91 amino acids
residue and have significant species differences in sequence
amino acids. The biological properties of β-lipotropin include fat-
mobilizing effect, corticotropic, melanocyte-stimulating and hy-
calcemic activity and, in addition, an insulin-like effect,
expressed in increasing the rate of glucose utilization in tissues.
It is assumed that the lipotropic effect occurs through the system
* The group of gonadotropins also includes the human chorionic gonadotropin
century (hCG), synthesized by placental cells and represented by a glycoprotein.
adenylate cyclase–cAMP–protein kinase, the final stage of action
which is the phosphorylation of inactive triacylglycerol lipase.
This enzyme, after activation, breaks down neutral fats into
diacylglycerol and higher fatty acid (see Chapter 11).
The listed biological properties are not due to β-lipotropic
nom, which turned out to be deprived of hormonal activity, and its products
decay formed during limited proteolysis. It turned out that
in the brain tissue and in the intermediate lobe of the pituitary gland, biological
chemically active peptides with opiate-like effects. Privo-
Let's look at the structures of some of them:
N–Shooting Range–Gli–Gli–Hairdryer–Meth–OH
Methionine-enkephalin
N–Shooting Range–Gli–Gli–Fen–Lei–ON
Leucine-enkephalin
N–Shooting Range–Gli–Gli–Hairdryer–Met-Tre-Ser-Glu-Liz-Ser-Gln-Tre-Pro-
Lei–Val–Tre–Lei–Fen–Liz–Asn–Ala–Ile–Val–Liz–Asn–Ala–Gis–
Liz–Liz–Gly–Gln–OH
β-Endorphin
The common type of structure for all three compounds is tetra-
peptide sequence at the N-terminus. It has been proven that β-endorphin (31
AMK) is formed by proteolysis from the larger pituitary
β-lipotropin hormone (91 AMK); the latter, together with ACTH, is formed from
common precursor - prohormone, called p o o p i o k o r t i n o m
(is, therefore, a preprohormone) having a molecular
weighing 29 kDa and containing 134 amino acid residues. Biosynthesis
and the release of proopiocortin in the anterior pituitary gland is regulated
corticoliberin of the hypothalamus. In turn, from ACTH and β-lipo-
tropin through further processing, in particular limited pro-
theolysis, α- and β-melanocyte-stimulating hormones are formed, respectively
monos (α- and β-MSH). Using DNA cloning techniques, as well as
Sanger method for determining the primary structure of nucleic acids
the nucleotide sequence was discovered in a number of laboratories
Proopiocortin precursor mRNA. These studies may serve
live as the basis for the targeted production of new biologically active
ny hormonal therapeutic drugs.
Below are peptide hormones formed from β-lipotro-
pin by specific proteolysis.
Plot β -lipotropin
Peptide hormone
γ-Lipotropin
Met-enkephalin
α-Endorphin
γ-Endorphin
δ-Endorphin
β-Endorphin
Considering the exclusive role of β-lipotropin as a precursor
of the listed hormones, we present the primary structure of β-lipotropin
pigs (91 amino acid residues):
N–Glu–Lei–Ala–Gly–Ala–Pro–Pro–Glu–Pro–Ala–Arg–Asp–Pro–Glu–
Ala–Pro–Ala–Glu–Gli–Ala–Ala–Ala–Arg–Ala–Glu–Lei–Glu–Tir–
Gli–Lei–Val–Ala–Glu–Ala–Glu–Ala–Ala–Glu–Liz–Liz–Asp–Glu–
Gly–Pro–Tyr–Lys–Met–Glu–Gis–Phen–Arg–Trp–Gly–Ser–Pro–Pro–
Liz–Asp–Lys–Arg–Tyr–Gly–Gly–Fen–Met–Tre–Ser–Glu–Lys–Ser–
Gln–Tre–Pro–Lei–Val–Tre–Lei–Fen–Liz–Asn–Ala–Ile–Val–Liz–
Asn-Ala-Gis-Lys-Lys-Gly-Gln-OH
Increased interest in these peptides, in particular enkephalins
and endorphins, is dictated by their extraordinary ability, like morphine,
relieve pain. This area of research is the search for new applications
native peptide hormones and (or) their directed biosynthesis is
interesting and promising for the development of physiology, neurobiology,
neurology and clinics.
HORMONES OF THE PARATHYROID GLANDS
(PARATE HORMONES)
Parathyroid hormone is also a protein hormone.
(parathyroid hormone), more precisely, a group of parathyroid hormones that differ in sequence
amino acid activity. They are synthesized by the parathyroid glands -
mi. As early as 1909, it was shown that removal of the parathyroid glands
causes tetanic convulsions in animals against the background of a sharp fall
plasma calcium concentrations; the introduction of calcium salts prevents
death of animals. However, only in 1925 from the parathyroid glands
an active extract was isolated that causes a hormonal effect -
in 1970 from the parathyroid glands of cattle; was then
its primary structure has been determined. It was found that parathyroid hormone synthesizes
comes in the form of a precursor (115 amino acid residues) pro p a r a t -
hormone, but the primary product of the gene turned out to be a pr e p r o p a r a t -
25 amino acid residues. The bovine parathyroid hormone molecule contains 84
amino acid residue and consists of one polypeptide chain.
It was found that parathyroid hormone is involved in the regulation of cation concentrations.
new calcium and associated phosphoric acid anions in the blood. How
It is known that the concentration of calcium in the blood serum is a chemical
constants, its daily fluctuations do not exceed 3–5% (normally 2.2–
2.6 mmol/l). The biologically active form is considered to be ionized
calcium, its concentration ranges from 1.1–1.3 mmol/l. Ions
calcium turned out to be essential factors that are not replaceable by others
cations for a number of vital physiological processes: muscle
contraction, neuromuscular excitation, blood clotting, penetration
resistance of cell membranes, activity of a number of enzymes, etc. That's why
any changes in these processes due to long-term deficiency
lump of calcium in food or a violation of its absorption in the intestines, lead
to enhance the synthesis of parathyroid hormone, which promotes the leaching
calcium salts (in the form of citrates and phosphates) from bone tissue and corresponding
This leads to the destruction of mineral and organic components of bones.
Another target organ of parathyroid hormone is the kidney. Parathyroid hormone decreases
reabsorption of phosphate in the distal tubules of the kidney and increases tubular
vuyu reabsorption of calcium.
It should be noted that in the regulation of Ca concentration
in the extracellular
three hormones play a major role in the fluid: parathyroid hormone, calcitonin,
] – derivative of D
(see chapter 7). All three hormones regulate levels
But their mechanisms of action are different. Thus, the main role of calcitriol
la is to stimulate calcium absorption
and phosphate in the intestines,
and against the concentration gradient, while parathyroid hormone
promotes their release from bone tissue into the blood and calcium absorption
in the kidneys and the excretion of phosphates in the urine. The role of calcitonin is less studied
in the regulation of Ca homeostasis
in organism. It should also be noted that
Calcitriol has a similar mechanism of action at the cellular level
the action of steroid hormones (see below).
It is considered proven that the physiological effect of parathyroid hormone on
kidney cells and bone tissue are realized through the adenylate cyclase-system
THYROID HORMONES
The thyroid gland plays an extremely important role in metabolism.
This is evidenced by a sharp change in basal metabolism observed
mine for disorders of the thyroid gland, as well as a number
indirect data, in particular its abundant blood supply despite
small weight (20–30 g). The thyroid gland consists of many
special cavities - follicles, filled with a viscous secretion - colloid.
The colloid contains a special iodine-containing glycoprotein with high
they say weighing about 650,000 (5000 amino acid residues). This glyco-
the protein was named i o d t i r e o g l o b u l i n a . He is
a reserve form of thyroxine and triiodothyronine - the main follicle hormones
cular part of the thyroid gland.
In addition to these hormones (the biosynthesis and functions of which will be considered,
see below), in special cells - the so-called parafollicular cells,
or C-cells of the thyroid gland, a peptide hormone is synthesized
childbirth, ensuring a constant concentration of calcium in the blood. He
called calcitonin. For the first time the existence of calcite
nin, which has the ability to maintain a constant level of cal-
tion in the blood, pointed out in 1962 by D. Kopp, who mistakenly believed that this
The hormone is synthesized by the parathyroid glands. Currently
Calcitonin is not only isolated in pure form from thyroid tissue
animals and humans, but also the 32-membered amino acid
sequence confirmed by chemical synthesis. Below is
on the primary structure of calcitonin obtained from the thyroid gland