牛补体第三成分的分离与特性分析

Isolation and characterization of the third component of bovine complement.

作者信息

Menger M, Aston W P

出版信息

Vet Immunol Immunopathol. 1985 Dec;10(4):317-31. doi: 10.1016/0165-2427(85)90021-2.

Abstract

C3 was obtained from bovine serum by polyethylene glycol precipitation and chromatography on DEAE-Sephadex A-50, CM-Sephadex A-50 and Sephacryl S-200. The protein has a molecular weight of 183,000 (alpha-chain 114,000 and beta-chain 69,000). A CVF-induced bovine C3 convertase (Sepharose-CVF.Bb) cleaved C3 into C3a (11,000) and C3b (172,000) as shown by SDS-polyacrylamide gel electrophoresis. Isoelectricfocusing of C3 demonstrated at least three electrophoretic variants with pI 6.55-6.85. The isolated protein promoted the formation and action of a C3 convertase in the presence of purified bovine factors B and D. A monospecific antiserum prepared in rabbits failed to cross react with human C3 or CVF. C3c was identified as a contaminant during the isolation of C3.

摘要

通过聚乙二醇沉淀以及在DEAE-葡聚糖凝胶A-50、CM-葡聚糖凝胶A-50和Sephacryl S-200上进行色谱分离，从牛血清中获得C3。该蛋白质的分子量为183,000（α链114,000，β链69,000）。如SDS-聚丙烯酰胺凝胶电泳所示，CVF诱导的牛C3转化酶（琼脂糖-CVF.Bb）将C3裂解为C3a（11,000）和C3b（172,000）。C3的等电聚焦显示至少有三种电泳变体，其pI为6.55 - 6.85。在纯化的牛因子B和D存在的情况下，分离出的蛋白质促进了C3转化酶的形成和作用。用兔制备的单特异性抗血清与人C3或CVF无交叉反应。在C3的分离过程中，C3c被鉴定为一种污染物。