Solubilization of IgG-binding proteins from group A and G streptococci.

The release of IgG-binding proteins from the cell surface of streptococcal strains AR-1 and G148 with various proteolytic enzymes, acid, alkali or SDS was investigated. The IgG-binding proteins were purified by affinity chromatography using IgG-Sepharose Fast Flow. After SDS-polyacrylamide gel electrophoresis and immuno-electroblotting the major proteins identified varied in relative molecular mass from 15,000 to 65,000 depending on the solubilizing agent used. The results showed that solubilization with trypsin gave the highest yield of IgG-binding proteins, that strain G148 yielded about twice the amount of protein as strain AR-1, and that elastase released an IgG-binding protein of high relative molecular mass of 65,000.