Interaction of bacterial Fc receptors with goat immunoglobulins.
The interaction of type I (staphylococcal protein A) and type III (streptococcal FcRc) bacterial Fc receptors with goat immunoglobulins has been studied. Staphylococcal protein A bound poorly to the majority of goat immunoglobulins at all pHs tested. There was some evidence that protein A bound IgG2 better than IgG1, particularly at pH 8 and above. One of 10 sera tested demonstrated a high level of reactivity with protein A and this was shown to correlate with the presence of a natural antibody to protein A. The streptococcal Fc receptors, FcRc, bound efficiently to all goat IgG and goat sera tested. Both goat IgG subclasses reacted efficiently with the FcRc between pH 6 and 8. Inhibition of binding of 125I-FcRc to immobilized goat IgG enabled levels of IgG in goat serum to be estimated. These results suggest the streptococcal FcRc will be of value as an immunochemical reagent in studies involving isolation and quantitation of goat immunoglobulins.
D000818:Animals; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D006041:Goats; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000145:classification / Q000276:immunology*; D011961:Receptors, Fc / Q000276:immunology*; D013205:Staphylococcal Protein A / Q000276:immunology*; D013291:Streptococcus / Q000276:immunology*
D007074:Immunoglobulin G; D011961:Receptors, Fc; D013205:Staphylococcal Protein A