MEDIUM MOLECULAR-WEIGHT FACTOR-X ACTIVATING ENZYME FROM VIPERA-BERUS-BERUS VENOM

被引：20

作者：

SAMEL, M ^{[1
]}

SIIGUR, J ^{[1
]}

机构：

[1] ESTONIAN ACAD SCI,INST CHEM PHYS & BIOPHYS,TALLINN,ESTONIA

来源：

TOXICON | 1995年 / 33卷 / 01期

关键词：

D O I：

10.1016/0041-0101(94)00143-V

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Vipera berus berus venom contains several factor X activating enzymes. One of them (VBFXAE) was separated by gel-filtration on Sephadex G-100 superfine and on a bacitracin-agarose column. The enzyme is a single-chain glycoprotein with mel. wt 38,000. The enzyme has several molecular forms with pI 3.5-4.5. After neuraminidase treatment the enzyme has pI 4.5. VBFXAE contains 2 Ca per mole. The activator is inactive on synthetic substrates, on casein, prothrombin, and fibrinogen, and appears to act specifically on factor X. The activator also weakly hydrolyses the insulin B-chain at the positions Ala(14)-Leu(15) and Tyr(16)-Leu(17). The cleavage of the insulin B-chain is inhibited by EDTA, suggesting the metalloproteinase nature of the enzyme.

引用

页码：41 / 52

页数：12

共 23 条

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