Biosynthesis of hemolybin.

. Hemoglolin(Hb) accounts for 95% of the total amount of
proteins
in red blood cells in mature red blood cells, which is the most important substance for blood transport of O2, and co2 delivery is also related. Hemoglobin is a tumogen of four sub-groups, each of which is made up of a molecule of globin and a molecule of hemoglobin (heme). Because the biosynthesis of globin is the same as that of a general protein, this section focuses on the biosynthesis of hemoglobin.hemoglobin is also a secondary to other proteins such as myoglobin, catalase, peroxidase, etc. As a result, hemolyin can be synthesized in general cells, and the synthesis path is the same. In human red blood cells, the synthesis of hemolybin begins with the early movement of red blood cells and continues to be synthesized until the meshing of red blood cells. Mature red blood cells no longer have hemolybin synthesis.(i) the synthesis path (process) of hemolyxinthe basic raw materials for hemolyxine synthesis are glycine, amber coenzyme A and Fe. The initial and final processes of synthesis are mitochondrials, while the intermediate stages are carried out in cell fluid. The synthesis process is divided into four steps: 1.δ-amino-γ-ketone-ketone acid (δ-aminplevulinic acid, ALA): in mitochondrials, ALA is first produced by the catalytic cogeneration of glycine and amber coenzyme A in ALA synthase (ALa synthetase). ALA synthase consists of two sub-base, each with a molecular weight of 60,000. Its coenzyme is phosphate acetaldehyde. This enzyme is a speed-limiting enzyme synthesized by hemolybin and is inhibited by hemolybin feedback.. 2. The generation of bilelin: mitochondrial-generated ALA enters the cell fluid, and under the catalysis of ALA dehydrase, the two-molecule ALA dehydration shrinks into a molecule gallbladgen (prophobiogenlin, PBG). ALA dehydrase consists of eight sub-base and has a molecular weight of 260,000. For -containing enzymes.. 3. The generation of urinary urethra and manure: In cell fluid, the four-molecule PBG deamination produces a molecule of uroporphyrinogen III. (uroporphyrinogen III., UPG III.). This reaction process requires two enzymes, uroporphyrinogen synthetase, also known as bileogen deaminase (PBG deaminase) and uroporphyrinogen III. cosynthase. First of all, PBG, under the action of urinary pyridoxygenase, de-ammonia shrinkation produces a line of quaterine. It is then catalyzed by urethra III. Isoenzyme, and cyclic to produce urinary urethra III. When there is no urethra III. isoenzyme, the line-shaped quid can be naturally cycled into urinary urethyl I. (UPG-I.), the difference between the two urethropoietics is: UPGI. 7th binding is acetic acid, 8th is acetate base, while UPg III. In contrast, the 7th position is acetate, the 8th bit is acetic acid. Normally UPG-III. and UPG-I. are 10000:1.A stands for acetic acid base, P stands for acetate-based ureurisic urethrogen III. Further catalysis by urethra III. de-sterilase, so that its four acetic acid (A) de-decontamination into methyl (M), thus generating fecal ethnoids III.coproporphyrinogen III., CPG III.).. 4. Hemolanin generation: the resulting manure in the cell fluid III. Then into the mitochondrials, under the action of the oxidation dexterase of the fecal radonogen, so that 2 and 4 bits of propylene acid (P) dehydrogenation to produce vinyl (V), the generation of the original pyrethrin IX. The dehydrogenation is catalyzed by the original IX oxidase, so that the methene-based oxidation connected to the four pyridoxine rings is oxidized into methyl, resulting in the original IX. Finally, hemoerin is produced by catalysis of ferrochelatase and Fe2 plus. (Figures 10-18).. A. Acetic P. propylene M. methyl V. vinylFigure 10-18 Biosynthesis of hemoglobin and its regulationHemoglobin is generated and transferred from mitochondrials to cytostic fluid, binding to globin to become hemoglobin. Normal adults synthesize 6 grams of Hb per day, equivalent to 210 mg of hemolyxin.(ii) the synthesis of hemolybinis regulated by a variety of factors, mainly regulating the generation of ALA.. 1.ALA synthase Hemolybin synthase system, ALA synthase is the speed limit enzyme, the smallest amount. Hemolybin has a feedback inhibition effect on this enzyme. It is believed that hemoglobin can bind to the inhibitor protein in the body to form an active inhibitor protein, thereby inhibiting the synthesis of ALA synthase. In addition, hemolybin also has a direct negative feedback to regulate the activity of ALA synthase. Experiments show that hemolybin concentration of 5×10-6M can inhibit the synthesis of ALA synthase, concentration of 10-5 to 10-4M can inhibit the activity of enzymes. Normally, hemoglobin is produced and binds to globin very quickly, but when hemoglobin is synthesized too much, too much hemoglobin is oxidized to high-speed hemoglobin (hematin), a strong inhibitor of ALA synthase, and can also inhibit the synthesis of ALA synthase.male
hormone
- Testosterone produces 5 beta-hydrogen testosterone under the action of 5 beta-reductase in the liver, which induces the production of ALA synthase, thereby promoting hemohemolysis production. Some
compounds
also induce ALA synthase, such as barbito, gray aflatoxin and other drugs, can induce the synthesis of ALA synthase.. 2. ALA dehydrase and ferrous chelation enzymes: ALA dehydrase and ferrous chelation enzymes are sensitive to heavy metals, such as lead poisoning can inhibit these enzymes and reduce hemoxigen synthesis. . 3. Hematopoirses
Growth Factor
: A variety of hematopoesic growth factors have been found, such as multi-series (multi) set of drop stimulation factors, neutral granulocyte-macrophage collection stimulation factor (GM-CSF), lecytokine 3 (IL-3), and erythocytosis. Erythropoiefin (EPO) plays a key role in the growth and differentiation of red blood cells. The human EPO
gene
located in chromosome 7 long arm area 21 and consists of four inclusions and five exons. The encoded
polypeptide
consists of 193
amino acids
residues. During the secretion process, the signal peptide is hydrolysed to become a mature peptide of 166 amino acids. The molecular weight is 18398. EPO is a glycoprotein consisting of peptides and glycosyl, with a total molecular weight of 34000. Sugar-based plays an important role in Epo synthesis in secretion and biological activity. In
serum
Epo is mainly synthesized by the kidneys, and fetuses and newborns are mainly synthesized by the liver. Kidney secretion of Epo increases when the volume of red blood cells in the circulating blood is reduced or the body is deprived of oxygen. Epo promotes the proliferation and differentiation of primitive red blood cells, accelerates the maturation of nuclear erythrin cells, and promotes the production of ALA synthase, thereby promoting hemolybin production. iron also promotes the synthesis of hemolybin. Hemoglobin also promotes the synthesis of globulin. caused by abnormal hemolybin anabolic disorders that cause the build-up of rickets compounds or their ex-bodies, known as porphyria. Congenital red blood cell-producing rickets (congenital erythropoietic porphyria) is due to a congenital lack of urethra III. isoenzyme, and the transformation of the line tetracycline to urinary urethra III. is blocked, resulting in an increase in urinary urethra I. generation. A large amount of urinary urethra I. and manure I. appeared in the patient's urine.
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