Abstract
Clostridium perfringensa-toxin obtained from a commercial source contained at least seven protein bands when examined by SDS polyacrylamide disc gel electrophoresis. The fraction with an Rm of 0.29–0.56 contained 95.6% of the total hemolytic activity and all of the phospholipolytic acitivity. The a-toxin when passed through a Sephadex G-100 column yielded several peaks but only one active fraction. This fraction upon electrophoresis in a SDS polyacrylamide disc gel system contained two protein bands. Only one protein with a Rm of 0.64 possessed hemolytic and phospholipolytic activites. A second passage of the active fraction through Sephadex G-100 yielded only one protein band. This protein exhibited both hemolytic and phospholipolytic activities. For C. perfringens, it is apparent that both of these activities reside with the same protein.
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