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在澳大利亚的毒蛇毒液中,凝血酶原酶样酶复合物的促凝适应。

Procoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom.

机构信息

Department of Pediatrics, Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, PA 19104, USA.

出版信息

Toxins (Basel). 2010 Jun;2(6):1554-67. doi: 10.3390/toxins2061554. Epub 2010 Jun 18.

Abstract

The macromolecular enzyme complex prothrombinase serves an indispensable role in blood coagulation as it catalyzes the conversion of prothrombin to thrombin, a key regulatory enzyme in the formation of a blood clot. Interestingly, a virtually identical enzyme complex is found in the venom of some Australian elapid snakes, which is composed of a cofactor factor Va-component and a serine protease factor Xa-like subunit. This review will provide an overview of the identification and characterization of the venom prothrombinase complex and will discuss the rationale for its powerful procoagulant nature responsible for the potent hemostatic toxicity of the elapid venom.

摘要

大分子酶复合物凝血酶原酶在血液凝固中起着不可或缺的作用,因为它催化凝血酶原转化为凝血酶,凝血酶是形成血栓的关键调节酶。有趣的是,在某些澳大利亚眼镜蛇的毒液中也发现了几乎相同的酶复合物,它由辅因子因子 Va 成分和丝氨酸蛋白酶因子 Xa 样亚基组成。本综述将概述毒液凝血酶原酶复合物的鉴定和特性,并讨论其强大的促凝性质的原理,这是眼镜蛇毒液具有强大止血毒性的原因。

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