Oglesby T J, Accavitti M A, Volanakis J E
Department of Medicine, University of Alabama, Birmingham 35294.
J Immunol. 1988 Aug 1;141(3):926-31.
We raised murine mAb against human C protein C2. The representative mAb 3A3.3 (IgG1 kappa) recognized an epitope on the C2b domain of C2, as determined by binding and inhibition of binding radioassays. The hemolytic activity of purified human C2 and of C2 in normal human serum was inhibited by the mAb. The rate of decay of the C3-convertase at 30 degrees C was not affected by the mAb. C2 binding to EAC4b was inhibited by intact IgG and the Fab fragment of the mAb; 50% inhibition required 1 microgram/ml of either. The data suggest the presence of a C4b-binding site on the C2b domain of C2 and that the mAb recognizes an epitope at, or adjacent to, this site. The C2b portion of the C2 molecule may be important in assembly of the classical pathway C3-convertase.
我们制备了针对人补体C2的鼠单克隆抗体。具有代表性的单克隆抗体3A3.3（IgG1 κ）识别C2的C2b结构域上的一个表位，这是通过结合和结合抑制放射性测定法确定的。纯化的人C2以及正常人血清中的C2的溶血活性均被该单克隆抗体抑制。30℃时C3转化酶的衰变速率不受该单克隆抗体影响。完整的IgG和该单克隆抗体的Fab片段均可抑制C2与EAC4b的结合；50%抑制率所需的二者浓度均为1微克/毫升。数据表明C2的C2b结构域上存在一个C4b结合位点，且该单克隆抗体识别此位点或其邻近的一个表位。C2分子的C2b部分可能在经典途径C3转化酶的组装中起重要作用。
