C1 subcomponent conplexes in normal and pathological sera studied by crossed immunoelectrophoresis.

Selected pathological sera gave three molecular species of C1s protein on crossed immunoelectrophoresis in the presence of calcium. C1s precipitates were obtained at the origin and in the beta1 and alpha2 regions. 12 normal sera gave C1s protein peaks at the origin and in alpha2 position. One of the normal sera also contained a small amount of the beta1 C1s protein. The C1s protein at the origin represented macromolecular C1. The alpha2 peak was a complex composed of C1 IA, C1s and C1r proteins. This complex was preformed in serum and did not show C4 cleaving activity. The molecular species in the beta1 region was shown to be a calcium-dependent complex of C1r and C1s, probably in proenzyme form. the C1r-C1s complex formed macromolecular C1 on addition of purified C1q to serum. During electrophoresis activation of C1 subcomponents was initiated by a mechanism involving CIr with generation of CIs activity in eluted fractions corresponding to the position of macromolecular C1 as well as in the beta region. The significance of beta1 C1s complexes or of alpha2 C1s complexes in normal and pathological sera was discussed.