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Yuji FUKUMOTO, Shinya INAI, Kazuyoshi NAGAKI, Kyoko IIDA, Eiji YAMAGAMI, Yasuhiko MASUHO, Tsuneo WATANABE, Interaction of S-Suffonated Human IgG with Human Complement and Its Components, The Journal of Biochemistry, Volume 82, Issue 4, October 1977, Pages 955–960, https://doi.org/10.1093/oxfordjournals.jbchem.a131799
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Abstract
S-sulfonated human IgG (S-sIgG) was prepared by treating IgG with sodium sulfite and sodium tetrathionate. The treatment resulted in the selective cleavage of interchain disulfide bonds of the IgG to give S-sulfonate groups. Complement fixing activities of aggregated S-sIgG and the immune complex formed with the S-sIgG antibody were very weak. S-sIgG at a high dose reduced the activity of the first complement component (C1) in normal human serum without any reduction of other complement components activites, but S-alkylated IgG at the same dose did not. Loss of C1 activity was not caused by either S-sulfonated myeloma proteins (IgA and IgE) or urea-treated S-sIgG, in which both inter- and intra-chain disulfide bonds were cleaved.
These results suggest that the selective reduction of C1 by S-sIgG is due to a conformational change of the immunoglobulin.