Binding of fragments of human IgG to solid-phase C3b measured by enzyme-linked immunosorbent assay (ELISA).
The binding of human IgG and different fragments of IgG to C3b adsorbed to polystyrene tubes has been studied by the enzyme-linked immunosorbent assay. Heat-denatured polyclonal IgG and F(ab')2 and Fab fragments of IgG bound to solid-phase C3b. Heat-denatured Fc fragments of IgG also had some reactivity with C3b, but at significantly higher concentrations than F(ab')2 and Fab fragments. The binding of heat-denatured IgG could not be completely inhibited by the addition of heat-denatured F(ab')2 fragments in tenfold excess. The results suggest that the binding of heat-denatured IgG to solid-phase C3b is mediated through the Fab and Fc portions of IgG molecules.
D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D003176:Complement C3 / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007128:Immunoglobulin Fragments / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D008970:Molecular Weight; D011485:Protein Binding
D003176:Complement C3; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G