Goers J W, Porter R R
Biochem J. 1978 Nov 1;175(2):675-84. doi: 10.1042/bj1750675.
Radioimmune assays were developed to assay the binding of complement components C1q, C1s and C4 to antibody aggregates and to cell-bound antibody. The binding of the components was compared with the haemolytic activity and with the capacity to form the C3 convertase activity in the presence of excess C2. The destruction of whole complement and of C4 activity is similar per 1,000 molecules of antibody in aggregates and cell-bound antibody, as is the binding of C1g and C1s, the latter being in a 1:2 molar ratio. The binding of C4 is about 12 times greater, per 1,000 molecules of antibody, on cells than in aggregates. However, the effective C4 molecules, as judged by the formation of C3 convertase activity, are much more similar on cells and aggregates. An assembly mechanism of the early components of complement on antibody-coated cells, which is compatible with these results, is suggested.
放射免疫测定法被开发用于检测补体成分C1q、C1s和C4与抗体聚集体以及细胞结合抗体的结合情况。将这些成分的结合情况与溶血活性以及在过量C2存在下形成C3转化酶活性的能力进行了比较。每1000个聚集体和细胞结合抗体中的抗体分子所导致的全补体破坏和C4活性破坏情况相似，C1g和C1s的结合情况也是如此，后者的摩尔比为1:2。每1000个抗体分子中，细胞上C4的结合量比聚集体中的大约大12倍。然而，根据C3转化酶活性的形成判断，细胞和聚集体上有效的C4分子更为相似。本文提出了一种与这些结果相符的补体早期成分在抗体包被细胞上的组装机制。
