人补体的第二个成分：其分离、被C'1酯酶裂解以及并入C'3转化酶。
The second component of human complement: its isolation, fragmentation by C'1 esterase, and incorporation into C'3 convertase.
作者信息
Polley M J, Müller-Eberhard H J
出版信息
J Exp Med. 1968 Sep 1;128(3):533-51. doi: 10.1084/jem.128.3.533.
Abstract
A method has been described for the purification and isolation of the second component of complement (C'2) from human serum. The protein is a beta(1)-globulin with an approximate molecular weight of 117,000. Immunochemical analysis using a variety of specific antisera, including a monospecific antiserum to the isolated protein, indicate that the C'2 protein represents a heretofore unrecognized human serum constituent. Isolated C'2 contained 2 x 10(9) "effective molecules" per microgram and 1000 hemolytically active C'2 molecules were required to produce a single hemolytically effective C'2 site on erythrocytes undergoing immune cytolysis. C'1 esterase treatment of C'2 resulted in reduction of both its electrophoretic mobility and its molecular size, the latter observation indicating fragmentation of the molecule. Direct evidence was presented for the physical presence of C'2 as an integral part of the enzyme C'3 convertase.
摘要
已描述了一种从人血清中纯化和分离补体第二成分（C'2）的方法。该蛋白质是一种β(1)-球蛋白，分子量约为117,000。使用多种特异性抗血清进行的免疫化学分析，包括针对分离出的蛋白质的单特异性抗血清，表明C'2蛋白代表一种迄今未被识别的人血清成分。分离出的C'2每微克含有2×10⁹个“有效分子”，并且在经历免疫细胞溶解的红细胞上产生单个溶血有效C'2位点需要1000个具有溶血活性的C'2分子。用C'1酯酶处理C'2会导致其电泳迁移率和分子大小降低，后一观察结果表明该分子发生了片段化。有直接证据表明C'2作为酶C'3转化酶的一个组成部分实际存在。
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