Inhibition of activated protein C by aprotinin and the use of the insolubilized inhibitor for its purification
| Autor: | J. Chabbat, O. Taby, M. Steinbuch |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
chemistry.chemical_classification
Chromatography Chemistry Elution Activator (genetics) Venom Hematology Prothrombin complex concentrate Amides Chromatography Affinity Chaotropic agent Enzyme Aprotinin Biochemistry Solubility medicine Humans Protease Inhibitors Blood Coagulation Tests Protein C medicine.drug |
| Zdroj: | Thrombosis research. 59(1) |
| ISSN: | 0049-3848 |
| Popis: | The study of the interaction between activated protein C (APC) and non-plasmatic inhibitors allowed us to demonstrate that aprotinin is a potent competitive inhibitor of APC with a Ki of 1.35 μmol/L. It was possible to adsorb immunopurified protein C (PC) activated by venom activator to insolubilized aprotinin and to recover the active enzyme after elution by HCl 0.1 Nor by a chaotropic ion, for example KSCN 3 mol/L. The interaction involved the active-site of the enzyme since PC and DIP-APC did not bind to the matrix. Thus, APC could be purified, after activation, in a one-stage procedure out of a mixture of protein such as a prothrombin complex concentrate. |
| Databáze: | OpenAIRE |
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