Biochemical characterization of fibrinogenolytic serine proteinases from Vipera lebetina snake venom

被引：25

作者：

Samel, M ^{[1
]}

Subbi, J ^{[1
]}

Siigur, J ^{[1
]}

Siigur, E ^{[1
]}

机构：

[1] NICPB, EE-12618 Tallinn, Estonia

来源：

TOXICON | 2002年 / 40卷 / 01期

关键词：

snake venom; vipera lebetina; alpha-fibrinogenase; beta-fibrinogenase; glycoprotein;

D O I：

10.1016/S0041-0101(01)00187-8

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Two glycosylated serine fibrinogenases isolated from Vipera lebetina venom have homologous N-terminal sequences and antigenic determinants but can be clearly differentiated according to substrate specificity, glycosylation levels, molecular mass and fibrinogen degradation. alpha -Fibrinogenase has no homolog among known serine proteinases. It has N-terminal similarity with snake venom arginine esterases but does not hydrolyze the esters of arginine, lysine and tyrosine. The enzyme has strong proteolytic activity and degrades alpha -chain of fibrinogen altering its clottability by thrombin. beta -Fibrinogenase is a typical arginine esterase which hydrolyzes esters and amides of arginine and attacks the beta -chain of fibrinogen. (C) 2001 Elsevier Science Ltd. All rights reserved.

引用

页码：51 / 54

页数：4

共 23 条

[1] THE FIBRIN PLATE METHOD FOR ESTIMATING FIBRINOLYTIC ACTIVITY [J].