The enzymes pepsin and trypsin act on... Digestion of proteins
In the form of an inactive precursor (proenzyme) trypsinogen. Trypsins from a number of animals were obtained in crystalline form (for the first time in 1932). The bovine trypsin molecule (molecular weight about 24 kDa) consists of 223 amino acid residues forming one polypeptide chain and contains 6 disulfide bonds. The isoelectric point of trypsin lies at 10.8, and the optimum of catalytic activity is at pH 7.8-8.0.
Trypsins belong to the group of serine proteases and contain serine and histidine residues in the active center. Trypsins easily undergo self-digestion (autolysis), which leads to contamination of trypsin preparations with inactive products (an industrial preparation contains up to 50% inactive impurities). High-purity trypsin preparations are obtained by chromatographic methods.
Physical properties
Trypsin is a colorless crystalline substance with a melting point of about 150.
Biological properties and functions
The main function is digestion. Catalyzes the hydrolysis of proteins and peptides. May be in an inactive state in the form of trypsinogen. It is activated, including by the intestinal enzyme enteropeptidase, by cleavage of the hexapeptide. It also catalyzes the hydrolysis of wax esters. The optimum catalytic activity is at 7.8-8. The active center is protein in nature and consists mainly of serine and histidine. Synthesized as trypsinogen in the pancreas and used in the intestines of mammals and fish. Converts other hydrolase proenzymes into active enzymes.
Application
Trypsin is used to make drugs. Trypsin preparations have anti-inflammatory and anti-edematous effects (when administered intravenously and intramuscularly); capable of selectively breaking down tissues that have undergone necrosis. In medicine, trypsin is used to treat wounds, burns, thrombosis, often in combination with other enzymes and antibiotics. Trypsin is part of drugs for systemic enzyme therapy - Wobenzyme, Phlogenzyme.
Literature
- Northrop D., Kunitz M., Herriott R. Crystal enzymes, trans. from English, M., 1950;
- Mosolov V.V.. Proteolytic enzymes, M., 1971.
- V. I. Struchkov, A. V. Grigoryan, V. K. Gostishchev, S. V. Lokhvitsky, L. S. Tapinsky Proteolytic enzymes in purulent surgery., M., 1970;
- Problems of medical enzymology" (edited by S. R. Mardashov). M., 1970;
- K. N. Veremeenko Proteolytic enzymes of the pancreas and their clinical use. Kyiv, 1967
- Systemic enzyme therapy. Experience and prospects / Ed. IN AND. Kulakova, V.A. Nasonova, V.S. Savelyeva.– St. Petersburg: Inter-Medica. 2004. – 264 p.
- Tets V.V., Knorring G.Yu., Artemenko N.K. and etc. The influence of exogenous proteolytic enzymes on bacteria // Antibiotics and chemotherapy. – 2004. – T. 49. – No. 12. – P. 9–13.
- Multienzyme drugs in purulent surgery: Guidelines / Ed. corresponding member RAMS N.A. Efimenko. – M., 2005. – 32 p.
Related enzymes
Trypsin's "closest relatives" are trypsinogen, pepsin, and chymotrypsin. Anionic analogues of trypsin have been found in higher animals, while neutral analogues have been found in many animals and plants.
Change in hydrolytic properties
Trypsin activity is suppressed by organophosphorus compounds, some metals, as well as a number of high-molecular protein substances - trypsin inhibitors, contained in the tissues of animals, plants and microorganisms. Ions 2+, 2+, 2+, 2+, 2+ increase the hydrolytic activity of trypsin.
Links
| Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21) | |
|---|---|
| Digestive enzymes | Enteropeptidase - Trypsin- Chymotrypsin - Elastase (Neutrophil, Pancreatic) |
| Coagulation | factors: Thrombin - Factor VIIa - Factor IXa - Factor Xa - Factor XIa - Factor XIIa - Kallikrein (PSA) fibrinolysis: Plasmin - Plasminogen activator (Tissue - Urokinase) |
| Complement system | Factor B - Factor D - Factor I - MASP (MASP1, MASP2) - C3 convertase |
| Others, immune system: | Himase - Granzyme - Tryptase - Proteinase 3/Myeloblastin |
| From biotoxins: | Ankrod - Batroxobin |
| Rest | Akrosin - Prolyl endopeptidase - Pronase - Proprotein convertase (1, 2) - Reelin - Subtilisin/Furin - Streptokinase - S1P - Cathepsin ( , ) |
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Synonyms:See what "Trypsin" is in other dictionaries:
- (Trypsinum). An endogenous proteolytic enzyme that breaks peptide bonds in a protein molecule. It also breaks down high molecular weight protein breakdown products, polypeptides such as peptones, as well as some low molecular weight peptides containing... ... Dictionary of medicines
TRYPSIN- TRYPSIN, an enzyme found in pancreatic juice, described by Kiihne in 1867, belongs to the group of proteases. It breaks down proteins, protamines, peptones and polypeptides. In its purest form, free from lipase and amylase, obtained by the method... ... Great Medical Encyclopedia
TRYPSIN- Trypsinum. Properties. Obtained from the pancreas of cattle. It is a white or white with a yellowish tint powder or odorless porous mass. Easily soluble in water and isotonic sodium chloride solution; pH 0.2% aqueous solution... Domestic veterinary drugs
Pancreatic enzyme that dissolves protein. Dictionary of foreign words included in the Russian language. Chudinov A.N., 1910. trypsin (gr. thrypsis liquefaction) is a digestive enzyme synthesized in the pancreas in the form of inactive... ... Dictionary of foreign words of the Russian language
TRYPSIN, a digestive enzyme secreted by the PANCREAS. It is released in an inactive form (so as not to damage tissue on the way to the intestine), then an enzyme in the small intestine converts it into active trypsin. Breaks down peptide bonds of amino acids... Scientific and technical encyclopedic dictionary
A digestive enzyme produced in the form of inactive trypsinogen by the pancreas of humans and animals; breaks down proteins in the intestines... Big Encyclopedic Dictionary
TRYPSIN, trypsin, pl. no, husband (from Greek tripsis grinding) (biol.). A substance in pancreatic juice that converts proteins into simpler, soluble compounds. Ushakov's explanatory dictionary. D.N. Ushakov. 1935 1940 ... Ushakov's Explanatory Dictionary
Proteolytic an enzyme synthesized by pancreatic cells in the form of an inactive precursor of trypsinogen. Activates pancreatic proenzymes and occupies a key position in digestion in the small intestine. In crystalline... ... Biological encyclopedic dictionary
Noun, number of synonyms: 4 drug (1413) protease (4) enzyme (253) ... Synonym dictionary
trypsin- One of the main digestive (proteolytic) enzymes, catalyzing the hydrolysis of peptides and other compounds at the site of bonds in which the carboxyl groups of arginine and lysine participate)
