MBL 相关丝氨酸蛋白酶（MASPs）的活性及其受天然抑制剂的调节。
Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors.
作者信息
Wong N K, Kojima M, Dobó J, Ambrus G, Sim R B
机构信息
Department of Biochemistry, University of Oxford, UK.
出版信息
Mol Immunol. 1999 Sep-Oct;36(13-14):853-61. doi: 10.1016/s0161-5890(99)00106-6.
There has been rapid progress in determining the mechanism by which complement is activated by the complex formed between Mannose-Binding Lectin and its associated proteases (MASPs). MBL and the MASPs are of low abundance, but are similar to the more abundant C1q-C1r2s2 complex (C1), which has been extensively investigated. In this review we summarise recent findings on MBL-MASPs' structure. enzymic activity and regulation, and compare MBL-MASPs with C1.
在确定甘露糖结合凝集素（MBL）与其相关蛋白酶（MASPs）形成的复合物激活补体的机制方面已取得了迅速进展。MBL和MASPs含量较低，但与已得到广泛研究的含量较高的C1q - C1r2s2复合物（C1）相似。在这篇综述中，我们总结了关于MBL - MASPs结构、酶活性和调节的最新发现，并将MBL - MASPs与C1进行比较。
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