ISOLATION AND CHARACTERIZATION OF TEXTARIN(R), A PROTHROMBIN ACTIVATOR FROM EASTERN BROWN SNAKE (PSEUDONAJA-TEXTILIS) VENOM

被引：23

作者：

STOCKER, K ^{[1
]}

HAUER, H ^{[1
]}

MULLER, C ^{[1
]}

TRIPLETT, DA ^{[1
]}

机构：

[1] BALL MEM HOSP, DEPT RES, MUNCIE, IN 47303 USA

来源：

TOXICON | 1994年 / 32卷 / 10期

关键词：

D O I：

10.1016/0041-0101(94)90352-2

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The venom of P. textilis contains two different enzymes which convert human prothrombin into thrombin. Prothrombin activation by Textarin, a serine proteinase containing a calcium-binding molecule site, with a molecular mass of 50,000 to 53,000 Da and I.P. 5.5, separated from crude venom by either barium citrate adsorption or hydroxyl apatite chromatography, is strongly stimulated by phospholipid and calcium ions. A second activator, found in the supernatant of barium citrate adsorbed venom solution, activates prothrombin in the absence of any co-factor. Human plasma coagulation induced by Textarin, phospholipid and calcium ions is affected by lupus anticoagulants. Textarin may thus be used for the detection of lupus anticoagulants in patient plasma samples.

引用

页码：1227 / 1236

页数：10

共 19 条

[1]

EXNER T, 1991, THROMB HAEMOSTASIS, V65, P320

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