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C1 SUBCOMPONENT COMPLEXES IN NORMAL AND PATHOLOGICAL SERA STUDIED BY CROSSED IMMUNOELECTROPHORESIS
Author(s) -
LAURELL ANNABRITA,
MÁRTENSSON ULLA,
SJÖHOLM ANDERS G.
Publication year - 1976
Publication title -
acta pathologica microbiologica scandinavica section c immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-1328
DOI - 10.1111/j.1699-0463.1976.tb00055.x
Subject(s) - immunoelectrophoresis , chemistry , macromolecule , electrophoresis , pathological , biochemistry , antibody , biology , medicine , immunology
Selected pathological sera gave three molecular species of C1s protein on crossed immunoelectrophoresis in the presence of calcium. Cls precipitates were obtained at the origin and in the β 1 and α 2 regions. 12 normal sera gave C1s protein peaks at the origin and in α 3 position. One of the normal sera also contained a small amount of the β 3 C1s protein. The Cls protein at the origin represented macromolecular C1. The α 2 peak was a complex composed of CI IA, C1s and C1r proteins. This complex was preformed in serum and did not show C4 cleaving activity. The molecular species in the β 1 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 C1r with generation of C1s activity in eluted fractions corresponding to the position of macromolecular C1 as well as in the β region. The significance of β 1 C1s complexes or of α 2 C1s complexes in normal and pathological sera was discussed.