Type-specific M antigen was extracted by heating type 1 group A streptococci at pH 2 in a boiling water bath. The protein was then purified by digestion with a preparation of crystalline ribonuclease which was free of proteolytic activity. It was further purified by fractional precipitation with (NH4)2SO4.
Elementary chemical analysis of the preparation thus obtained showed an absence of phosphorus and a sulfur content of 2.46 per cent. In the ultraviolet the maximum absorption was at a wave length of 276 mµ and the minimum at 255 mµ.
In electrophoresis experiments the preparation showed a single peak in the pH range of 3 to 9, but considerable boundary spreading was observed. The type 1 M antigen was isoelectric at pH 5.3 in sodium acetate buffer of ionic strength 0.1.
The serological reactivity of the protein isolated was typical of type 1 M antigen. This protein induced the formation in rabbits of type-specific precipitins and protective antibodies. The absorption of type 1 antibacterial serum with the purified M antigen removed both the protective antibodies and the type-specific precipitins from the serum.