Interaction of C3 and C3b with immunoglobulin G.
Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different. As a functional consequence of C3-IgG interaction, C3 binding was found to inhibit the specific precipitation of an IgG antibody preparation.
D000818:Animals; D000936:Antigen-Antibody Complex / Q000378:metabolism; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D003176:Complement C3 / Q000378:metabolism*; D003179:Complement C3b / Q000378:metabolism*; D006801:Humans; D007128:Immunoglobulin Fragments / Q000276:immunology; D007074:Immunoglobulin G / Q000378:metabolism*; D011817:Rabbits; D011863:Radioimmunoassay; D012995:Solubility
D000936:Antigen-Antibody Complex; D003176:Complement C3; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D003179:Complement C3b