An anticoagulant serine protease from the wasp venom of Vespa magnifica
An anticoagulant serine protease from the wasp venom of Vespa magnifica
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来自黄蜂毒液的抗凝血丝氨酸蛋白酶
DOI：
10.1016/j.toxicon.2008.01.002
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发表时间：
2008-04-01
期刊：
影响因子：
2.8
通讯作者：
Meng, Qingxiong
中科院分区：
文献类型：
--
作者：
Han, Junyou;You, Dewen;Meng, Qingxiong
黄蜂是一种重要的能致人死亡的有毒动物。凝血功能障碍是大量黄蜂蜇伤后的临床症状，但导致中毒表现的原因尚不清楚。本文采用Sephadex G-75凝胶过滤、CM-Sephadex C-25阳离子交换和快速蛋白液相色谱（FPLC）等方法对大黄蜂（Vespa magnifica, Smith）毒液中的一种毒素蛋白进行了纯化和表征。这种蛋白质被称为magnvesin。含有丝氨酸蛋白酶样活性，抑制血液凝固。编码magnvesin的cDNA是从胡蜂的毒液囊cDNA文库中克隆出来的。该蛋白由305个氨基酸残基组成。Magnvesin与来自黄蜂Polistes dominulus的过敏原丝氨酸蛋白酶具有52%的同源性。Magnvesin通过水解凝血因子TF， VII， VIII， IX和x发挥其抗凝血功能(c) 2008 Elsevier Ltd.。版权所有。
Wasp is an important venomous animal that can induce human fatalities. Coagulopathy is a clinical symptom after massive wasp stings, but the reason leading to the envenomation manifestation is still not known. In this paper, a toxin protein is purified and characterized by Sephadex G-75 gel filtration, CM-Sephadex C-25 cationic exchange and fast protein liquid chromatography (FPLC) from the venom of the wasp, Vespa magnifica (Smith). This protein, named magnvesin. contains serine protease-like activity and inhibits blood coagulation. The cDNA encoding magnvesin is cloned from the venom sac cDNA library of the wasp. The deduced protein from the cDNA is composed of 305 amino acid residues. Magnvesin shares 52% identity with allergen serine protease from the wasp Polistes dominulus. Magnvesin exerted its anti-coagulant function by hydrolyzing coagulant factors TF, VII, VIII, IX and X. (c) 2008 Elsevier Ltd. All rights reserved.