Existence of disulfide-bonded IgM-IgA, IgM-IgG and IgM-IgG fragment complexes in one patient

The existence of disulfide-bonded immunoglobulin (Ig) complexes of IgM-IgA, IgM-IgG, and IgM-IgG, in addition to a monoclonal IgM (kappa) paraprotein, free kappa chains and fragments of IgG (FIgG), were found in the plasma of a multiple gammopathy patient. This is the first report on the interclass disulfide-bonded Ig complexes. Upon exposure to a dissociating buffer containing 6 M urea, 0.1 M Tris-HCl, pH 8.0, a small portion of the IgM-IgA complexes and most of the IgM-IgG as well as the IgM-FIgG complexes dissociated, but the majority of the IgM-IgA and small amounts of other complexes remained intact. These intact complexes were not the result of antigen-antibody reactions and were apparently held together by disulfide bonds which could be broken into monomeric Ig basic units (H-L)2 and smaller components by mild reduction and alkylation.