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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.
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.