Biochemical and Hemostatic Mechanism of A Novel Thrombin-Like Enzyme

被引：23

作者：

Tang, Song-Shan ^{[1
]}

Zhang, Juan-Hui ^{[1
]}

Tang, Bai-Shan ^{[1
]}

Tang, Zhi-Hua ^{[1
]}

Li, Hong-Zhi ^{[1
]}

Yuan, Hao-Jia ^{[1
]}

Chui, Shu-Lian ^{[1
]}

Zhao, Er-Yao ^{[1
]}

机构：

[1] Guangdong Pharmaceut Univ, Dept Biochem & Mol Biol, Sch Basic Courses, Guangzhou 510006, Guangdong, Peoples R China

来源：

THROMBOSIS RESEARCH | 2009年 / 124卷 / 05期

关键词：

Agkistrodon acutus snake venom; Thrombin-like enzyme; Coagulant; Agacutin; Hemostasis; Blood coagulation; AGKISTRODON-ACUTUS VENOM; GLYCOPROTEIN IB ANTAGONIST; PURIFICATION;

D O I：

10.1016/j.thromres.2009.06.022

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Thrombin-like enzyme (TLE) plays a significant role in vessel injury hemostasis. A novel snake venom TLE (Agacutin) was purified from Agkistrodon Acutus snake venom. Structural analysis indicated that Agacutin is a heterodimer that has a MW of 29,402 Da, a pI value of 5.39, and optimum activity at 35 degrees C and pH 7.5. The N-terminal 15 amino acid sequences of Agacutin are DSSGWSSYEGHEYYV (small subunit) and DCSSGWSSYEEHQYY (large subunit). In vitro studies indicated that the coagulation activity of Agacutin was activated by Ca+2 or inhibited by phenylmethanesulfonyl fluoride, but not influenced by heparin or hirudin. The arginine esterase activity and fibrinogen hydrolysis result showed that Agacutin only cleaves alpha-subunit and releases fibrinopeptide A. In vivo studies indicated that Agacutin iv (0.01-0.05 U/kg) shortened 30.2-49% of the rabbit blood clotting time, or ip (0.5-2.0 U/kg) shortened 29.7-73.1% of the mouse tail bleeding time. Agacutin does not influence APTT, platelet or euglobulin clotting time, and activate Factor II or XIII. It converts fibrinogen into the soluble fibrin that accelerates hemostasis at wound. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：631 / 639

页数：9

共 20 条

[1] Snake venom proteins acting on hemostasis [J].