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牛补体第四成分C4的纯化与特性分析

The purification and characterization of bovine C4, the fourth component of complement.

作者信息

Booth N A, Campbell R D, Fothergill J E

出版信息

Biochem J. 1979 Mar 1;177(3):959-65. doi: 10.1042/bj1770959.

Abstract

The fourth component of complement, C4, was isolated from bovine plasma in high yield, by using simple purification techniques. The protein, like human component C4, is a beta-globulin with a mol.wt. of about 200 000 and consists of three polypeptide chains, alpha, beta and gamma, with apparent mol. wts. of 98 000, 82 000 and 32 000 respectively. The chains of C4 have been separated by methods previously used for human C4. Their amino acid compositions are very similar to those of the human component, but differences in carbohydrate distribution have been observed. The haemolytic activity of bovine C4 is totally destroyed by incubation with bovine C1s, the activated subcomponent of the first component of complement. Component C4, treated in this way, was shown to be cleaved in the alpha chain, which was decreased in mol.wt. by about 9000, corresponding to the removal of subcomponent C4a.

摘要

补体的第四成分C4,通过简单的纯化技术从牛血浆中高产率地分离出来。该蛋白质与人类成分C4一样,是一种分子量约为200000的β球蛋白,由三条多肽链α、β和γ组成,其表观分子量分别为98000、82000和32000。C4的这些链已通过先前用于人类C4的方法分离出来。它们的氨基酸组成与人类成分非常相似,但在碳水化合物分布上存在差异。牛C4的溶血活性在与补体第一成分的活化亚成分牛C1s孵育后完全被破坏。以这种方式处理的C4成分在α链中被裂解,其分子量降低了约9000,这与C4a亚成分的去除相对应。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f1db/1186463/89936c12f8a6/biochemj00469-0201-a.jpg

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