Nonaka M, Iwaki M, Nakai C, Nozaki M, Kaidoh T, Nonaka M, Natsuume-Sakai S, Takahashi M
J Biol Chem. 1984 May 25;259(10):6327-33.
The present paper describes the purification and characterization of a major serum protein of the rainbow trout (Salmo gairdneri) required for complement-related functions (target cell lysis and opsonization). This protein, termed C3-1, was identified as the third component (C3) of rainbow trout complement. It is homologous to component C3 of human and other mammalian complements based on its structural and functional characteristics. Rainbow trout C3-1 is a beta-globulin of Mr = 190,000 composed of two polypeptide chains (Mr = 128,000 alpha-chain and Mr = 74,000 beta-chain) linked by disulfide bonds. The chain structure of C3-1 is, therefore, very similar to those of the third and fifth components of mammalian complement. C3-1 retains, on its alpha-chain, a unique hidden thiol site that can be exposed upon attachment of methylamine in the same way as human C3 and C4. The amino acid composition and NH2-terminal sequence of C3-1 show significant homology to mammalian C3 and to cobra venom factor (cobra C3).
本文描述了虹鳟鱼(Salmo gairdneri)血清中一种主要蛋白质的纯化及特性,该蛋白质参与补体相关功能(靶细胞裂解和调理作用)。这种蛋白质被称为C3-1,被鉴定为虹鳟鱼补体的第三成分(C3)。基于其结构和功能特征,它与人类及其他哺乳动物补体的C3成分同源。虹鳟鱼C3-1是一种分子量为190,000的β球蛋白,由两条通过二硫键连接的多肽链组成(α链分子量为128,000,β链分子量为74,000)。因此,C3-1的链结构与哺乳动物补体的第三和第五成分非常相似。C3-1在其α链上保留了一个独特的隐蔽巯基位点,该位点在与甲胺结合时可以像人类C3和C4一样暴露出来。C3-1的氨基酸组成和NH2末端序列与哺乳动物C3和眼镜蛇毒因子(眼镜蛇C3)具有显著的同源性。