Anticoagulant Mechanism of Factor IX/factor X-binding Protein Isolated from the Venom of Trimeresurus flavoviridis

被引：11

作者：

Ishikawa, Midori ^{[1
]}

Kumashiro, Makoto ^{[1
]}

Yamazaki, Yasuo ^{[1
]}

Atoda, Hideko ^{[1
]}

Morita, Takashi ^{[1
]}

机构：

[1] Meiji Pharmaceut Univ, Dept Biochem, Tokyo 2048588, Japan

来源：

JOURNAL OF BIOCHEMISTRY | 2009年 / 145卷 / 01期

关键词：

FACTOR-IX; BLOOD-COAGULATION; GLA DOMAIN; CRYSTAL-STRUCTURE; FACTOR-VA; PROTHROMBINASE; COMPLEX; SNAKE; PURIFICATION; ACTIVATION;

D O I：

10.1093/jb/mvn145

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：

Anticoagulant mechanism of the coagulation factor IX/factor X-binding protein (IX/X-bp) isolated from the venom of Trimeresurus flavoviridis was investigated. IX/X-bp had no effect on the amidase activity of factor Xa measured with a synthetic peptide substrate Boc-Leu-Gly-Arg-pNA. Prothrombin activation by factor Xa without cofactors, such as factor Va and phospholipids, was only slightly influenced by IX/X-bp. However, prothrombin activation by factor Xa in the presence of factor Va resulted in IX/X-bp inhibiting the increase of k(cat) of thrombin formation through inhibition of interaction between factor Xa and factor Va. IX/X-bp also inhibited the decrease of K-m for thrombin formation through interaction with phospholipids. Thus, IX/X-bp appears to act as an anticoagulant protein by inhibiting the interaction between factor Xa and its cofactors in the prothrombinase complex by binding to the Gla domain of factor Xa.

引用

页码：123 / 128

页数：6

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