Interaction of Bothrojaracin with Prothrombin
| Autor: | Bianconi Ml, Robson Q. Monteiro, Russolina B. Zingali |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Binding Sites
Bothrops jararaca biology Chemistry Complex formation Thrombin Anticoagulants Venom Hematology biology.organism_classification Oxyuranus scutellatus Biochemistry Prothrombinase Physiology (medical) Zymogen activation Zymogen Crotalid Venoms Animals Humans Drug Interactions Prothrombin Bothrojaracin |
| Zdroj: | Pathophysiology of Haemostasis and Thrombosis. 31:273-278 |
| ISSN: | 1424-8840 1424-8832 |
| DOI: | 10.1159/000048073 |
| Popis: | Bothrojaracin (BJC) is a 27-kD protein from Bothrops jararaca venom that interacts with α-thrombin (KD = 0.7 nM) through both anion-binding exosites I and II. Recently, it has been shown that BJC interacts with the exosite I precursor (proexosite I) on human prothrombin (KD = 75 nM), forming a 1:1 Ca2+-independent noncovalent complex with the zymogen. Complex formation was associated with inhibition of zymogen activation by Oxyuranusscutellatus venom. In addition, BJC strongly decreased the prothrombin activation by factor Xa only in the presence of factor Va. A similar effect was observed in the presence of phospholipids, suggesting that BJC specifically inhibits the interaction of prothrombin with factor Va. It is proposed that BJC has two independent mechanisms for anticoagulation: (1) inhibition of exosite-I-dependent activities on α-thrombin, and (2) inhibition of prothrombin activation through interaction with proexosite I. |
| Databáze: | OpenAIRE |
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