[Anticoagulative and anticomplementary activity of endogenous inhibitor preparation from hepatopancreas of red king crab (Paralithosed camtschaticus) towards human blood]
| Autor: | Rudenskaia IuA, L. V. Kozlov, Liutova Lv, Rudenskaia Gn, S. S. Andina, M. V. Balashova, Isaev Va |
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| Rok vydání: | 2012 |
| Předmět: |
Proteases
animal structures Serine Proteinase Inhibitors Hepatopancreas Serpin Binding Competitive General Biochemistry Genetics and Molecular Biology C1-inhibitor Serine Non-competitive inhibition Thrombin Complement C1 medicine Animals Humans Fibrinolysin Blood Coagulation Serpins chemistry.chemical_classification biology Heparin Anticoagulants General Medicine Anatomy carbohydrates (lipids) Enzyme Biochemistry chemistry embryonic structures biology.protein Anomura medicine.drug Cysteine |
| Zdroj: | Biomeditsinskaia khimiia. 58(2) |
| ISSN: | 2310-6972 |
| Popis: | Serpins (SERine Protease INhibitors) - is large and diverse group of proteins with similar structures, which can inhibit both serine and cysteine proteases by an irreversible suicide mechanism. A novel serpin from hepatopancreas of Red King Crab (Paralithosed camtschaticus) was obtained and was studied its effect on the process of human blood plasma clotting. The investigated serpin shows a noticeable anticoagulative activity, which increases dramatically in the combined action with heparine. Though the inhibitor has almost no effect on thrombin, it inhibits C1s (C1-esterase). We studied the action of the serpin from P. camtschaticus on C1s via its competitive inhibition by C1 inhibitor and the novel enzyme. The calculated inhibition constant of the serpin from P. camtschaticus towards C1s is 2,02±0,71 М. Unlike C1 inhibitor, the novel serpin from P. camtschaticus doesn`t suppress fibrinolysis and at the same time prevents blood clotting. These features may be of interest for medical purposes. |
| Databáze: | OpenAIRE |
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