PURIFICATION AND CHARACTERIZATION OF LEBETASE, A FIBRINOLYTIC ENZYME FROM VIPERA-LEBETINA (SNAKE) VENOM

被引：83

作者：

SIIGUR, E

SIIGUR, J

机构：

[1] Laboratory of Bioorganic Chemistry, Institute of Chemical Physics and Biophysics, the Estonian Academy of Sciences

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1991年 / 1074卷 / 02期

关键词：

PROTEINASE; FIBRINOLYTIC ENZYME; SNAKE VENOM; (V-LEBETINA);

D O I：

10.1016/0304-4165(91)90156-B

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An anticoagulant proteinase, lebetase, was isolated from the venom of Vipera lebetina by gel filtration and anion-exchange chromatography. The proteinase consists of a single polypeptide chain with a molecular weight of 23 700. Amino acid analysis indicates that lebetase contains 214 residues. It consists of several isoforms in the pH range 4.6-5.4, all having fibrinolytic activity. Lebetase hydrolyzes casein, fibrinogen and fibrin, and oxidized insulin B-chain in the positions Ala14-Leu15 and Tyr16-Leu17 . Its fibrinolytic activity is inhibited by EDTA and lost upon heating at 70-degrees-C for 10 min. The enzyme readily hydrolyzes the A-alpha-chain and more slowly the B-beta-chain of fibrinogen. In fibrin, the same chains are attacked. Thus, the enzyme is an A-alpha, B-beta-fibrinogenase. The fibrinolytic activity of lebetase is direct, without anx plasminogen activation. E280(1%) is 13.0 for lebetase. The enzyme showed low hemorrhagic activity.

引用

页码：223 / 229

页数：7

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