CHEMICAL MODIFICATION AND CHARACTERIZATION OF ENTEROTOXIN FROM CLOSTRIDIUM PERFRINGENS TYPE A

Abstract

Enterotoxin from Clostridium perfringens type A has been purified. The enterotoxin was shown to be heat-labile, but re-activation of heat treated enterotoxin did occur down to an activity of 15 per cent of the native enterotoxin. The molecular weight was shown to be 34,000 by ultracentrifugation, and the molecular weight did not change significantly after treatment with 0.1 M β-mercaptoethanol and 6 M guanidine hydrochloride. It was concluded that the enterotoxin consists of one single polypeptide chain. The enterotoxin did not lose any activity after treatment with iodoacetic acid and iodoacetamide, but a complete loss of activity was observed after succinylation.