The lysis of cell walls of hemolytic streptococci by a phage-associated lysin has been described. A method is presented for preparing the lysin from Group C streptococcal phage lysates.

Following lysis almost all of the cell wall carbohydrate is recovered in solution. This material has the serological reactivity, physical-chemical properties, and values for nitrogen, rhamnose, and glucosamine similar to those of the carbohydrate isolated from the cell walls by the Streptomyces albus enzyme. Group C carbohydrate isolated by either enzyme inactivates Group C bacteriophage.

The protein liberated by the lysin from Group A Type 6 cell walls gives a type-specific precipitin reaction with homologous rabbit antiserum. Preliminary data are presented on the ammonium sulfate fractionation and the electrophoretic separation of a protein fraction with the serological reactivity of M protein.

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