补体系统
毒液
补体因子B
蛇毒
金属蛋白酶
生物化学
生物
替代补体途径
C3转化酶
补体成分2
等电点
糖蛋白
分子生物学
化学
基质金属蛋白酶
抗体
酶
免疫学
出处
期刊:Toxicon
[Elsevier]
日期:2010-12-01
卷期号:56 (8): 1459-1469
被引量:36
标识
DOI:10.1016/j.toxicon.2010.08.013
摘要
The complement system is a very important part of the immune system. Many snake venoms possess activities that influence the complement. A new metalloproteinase (termed atrase B) with anticomplementary activity was purified from Naja atra venom. Atrase B is a single chain glycoprotein with a molecular mass of 49.4 kDa and an isoelectric point of 9.7. Its N-terminal sequence shows high homology to those of metalloproteinases from cobra venoms. The cDNA sequence reveals that atrase B is a PIII class metalloproteinase. Atrase B slowly cleaves the Aα chain of fibrinogen. It also exhibits edema-inducing activity, but has no hemorrhagic activity and proteolytic activity against fibrin, azocasein, and N-benzoyl-l-arginine ethyl ester. Interestingly, atrase B inhibits activation of the complement classical and alternative pathways in a dose- and time-dependent manner. Complement components factor B and C6 are major targets for atrase B to cleave. Atrase B is the first identified SVMP that cleaves complement components factor B, C6, C7, and C8.
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