Cloning and characterization of a blood coagulation factor IX-binding protein from the venom of Trimeresurus stejnegeri

被引：23

作者：

Lee, WH

Zhuang, QY

Zhang, Y

机构：

[1] Chinese Acad Sci, Kunming Inst Zool, Dept Anim Toxinol, Kunming 650223, Yunnan, Peoples R China

[2] Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China

来源：

TOXICON | 2003年 / 41卷 / 07期

关键词：

snake venom; C-type lectin-like protein; coagulation FIX-binding protein; Trimeresurus steinegeri; cDNA sequence;

D O I：

10.1016/S0041-0101(03)00029-1

中图分类号：

R9 [药学];

学科分类号：

1007 [药学];

摘要：

A blood coagulation factor IX-binding protein (TSV-FIX-BP) was isolated from the snake venom of Trimeresurus stejnegeri. On SDS-polyacrylamide gel electrophoresis, TSV-FIX-BP showed a single band with an apparent molecular weight of 23,000 under non-reducing conditions. and two distinct bands with apparent molecular weights of 14,800 and 14,000 under reducing conditions. cDNA clones containing the coding sequences of TSV-FIX-BP were isolated and sequenced to determine the structure of the precusors of TSV-FIX-BP subunits. The deduced amino acid sequences of two subunits of TSV-FIX-BP were confirmed by N-terminal protein sequencing and trypsin-digested peptide mass fingerprinting. TSV-FIX-BP was a nonenzymatic C-type lectin-like anti-coagulant. The anti-coagulant activity of TSV-FIX-BP was mainly caused by its dose dependent interaction with blood coagulation factor IX but not with blood coagulation factor X. (C) 2003 Elsevier Science Ltd. All rights reserved.

引用

页码：765 / 772

页数：8

共 19 条

[1]

Bothrojaracin: A potent two-site-directed thrombin inhibitor [J].