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  • Book
    Heinz Luellmann, Klaus Mohr, Lutz Hein ; with 174 color plates by Juergen Wirth.
    Digital Access Thieme MedOne Education 2018
  • Article
    Fukumoto Y, Inai S, Nagaki K, Iida K, Yamagami E, Masuho Y, Watanabe T.
    J Biochem. 1977 Oct;82(4):955-60.
    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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