C3c and C3d fragments of human C3 bind myeloma IgG1 and IgG3 proteins.
Eight human myeloma proteins, two of each IgG subclass, were studied for binding to solid-phase C3c and C3d by the ELISA technique. Myeloma IgG1 kappa, IgG1 lambda, IgG3 kappa and IgG3 lambda proteins bound to C3c and C3d, while two IgG2 kappa, and two IgG4 kappa proteins failed to show significant binding affinity. The results suggest that like C1q, the stable binding sites of C3, located on the C3c and C3d parts of the molecule, have affinity for IgG subclasses 1 and 3.
D000818:Animals; D001667:Binding, Competitive; D055598:Chemical Phenomena; D002621:Chemistry; D003176:Complement C3 / Q000378:metabolism*; D015932:Complement C3c; D015933:Complement C3d; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D009194:Myeloma Proteins / Q000378:metabolism*; D011817:Rabbits; D011951:Receptors, Complement
D003176:Complement C3; D007074:Immunoglobulin G; D009194:Myeloma Proteins; D011951:Receptors, Complement; D015932:Complement C3c; D015933:Complement C3d