M antigens of group A streptococci isolated by means of immunochromatography. Biochemical and serological properties.

M proteins of Streptococcus pyogenes types 1 and 12 were purified by immunochromatography on immobilized type-specific opsonizing antibodies. The M proteins were characterized serologically and biochemically. They absorb after immobilization opsonizing antibodies and only precipitate with homologous antisera in immunodiffusion. In SDS PAGE they show one main band, corresponding to mol. weights of 5 X 104 (type 1) and 5.4 X 104 (type 12), accompanied by faint lines, which form with the main band a precipitation line of identity in SDS-crossed immunoelectrophoresis. Both M proteins aggregate blood platelets and clot fibrinogen.