A novel high molecular weight metalloproteinase cleaves fragment F1 of activated human prothrombin
Data(s) |
2004
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Resumo |
A hemorrhagic proteinase, jerdohagin, was purified from Trimeresurus jerdonii venom by gel filtration and ion-exchange chromatographies. It was a single chain polypeptide with an apparent molecular weight of 96 kDa as estimated by SDS-PAGE under the non-reducing and reducing conditions. Internal peptide sequencing indicated that it consisted of metalloproteinase, disintegrin-like and cysteine-rich domains and belonged to the class III snake venom metalloproteinases (class P-III SVMPs). Like other typical metalloproteinases, hemorrhagic activities of jerdohagin were completely inhibited by EDTA, but not by PMSF. Jerdohagin preferentially degraded a-chain of human fibrinogen. Interestingly, jerdohagin did not activate human prothrombin, whereas it cleaved human prothrombin and fragment F1 of activated human prothrombin. (C) 2004 Elsevier Ltd. All rights reserved. |
Identificador | |
Direitos |
A novel high molecular weight metalloproteinase cleaves fragment F1 of activated human prothrombin |
Fonte |
Chen, RQ; Jin, Y; Wu, JB; Zhou, XD; Li, DS; Lu, QM; Wang, WY; Xiong, YL.A novel high molecular weight metalloproteinase cleaves fragment F1 of activated human prothrombin,44,281-287,(SCI-E ): |
Palavras-Chave | #Pharmacology & Pharmacy; Toxicology |
Tipo |
期刊论文 |