Studies on ϵ-prototoxin of Clostridium perfringens type D

摘要: Abstract Clostridium perfringes type D was grown in protein-free medium. ϵ-Prototoxin found to contain insignificant amounts of ϵ-toxin. Purification ϵ-prototoxin by column chromatography on DEAE-cellulose followed CM-cellulose revealed multiple forms which differed their electrophoretic mobility but were immunochemically indistinguishable. The varied activation ratios and specific activities. most potent preparation contained 3 × 10 6 4.2 MLD/mg protein formed three electrophoretically different yet indistinguishable bands. Activation toxin treatment with trypsin resulted a more negatively charged molecule, suggesting splitting basic peptide (s). ϵ-toxin show complete immunologic identity.