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Interaction of S-sulfonated human IgG with human complement and its components.

Y Fukumoto·S Inai·K Nagaki·K Iida·E Yamagami·Y Masuho·T Watanabe
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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.

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Complement Fixation TestsComplement System ProteinsDisulfidesHemolysisHumansImmunoglobulin GPepsin ASulfonic AcidsJournal Article

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BibTeXRIS

Y Fukumoto, S Inai, K Nagaki, K Iida, E Yamagami, Y Masuho, T Watanabe. 1977. Interaction of S-sulfonated human IgG with human complement and its components.. https://doi.org/10.1093/oxfordjournals.jbchem.a131799

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