Affinity chromatography purification of Clostridium perfringens enterotoxin

Abstract

Anti enterotoxin immunoglobulins immobilized on CH Sepharose or CNBr Sepharose were used for affinity chromatography purification of Clostridium perfringens enterotoxin. Cell extracts containing enterotoxin or partially purified toxin preparations were applied to the column and nonspecifically bound protein was eluted. NaOH was used to elute specifically bound toxin. The purity of enterotoxin purified by Sephadex G 100 chromatography followed by affinity chromatography appears similar to toxin highly purified by conventional means. The procedure can be used successfully for the rapid (less than 2 hr) purification of small amounts of enterotoxin.