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- W1483281977 abstract "Clostridium perfringes type D was grown in protein-free medium. ϵ-Prototoxin was found to contain insignificant amounts of ϵ-toxin. Purification of ϵ-prototoxin by column chromatography on DEAE-cellulose followed by CM-cellulose revealed multiple forms of ϵ-prototoxin which differed in their electrophoretic mobility but were immunochemically indistinguishable. The multiple forms of ϵ-prototoxin varied in their activation ratios and specific activities. The most potent preparation contained 3 × 106 to 4.2 × 106 MLD/mg protein which was formed of three electrophoretically different yet immunochemically indistinguishable bands. Activation of ϵ-prototoxin to toxin by treatment with trypsin resulted in a more negatively charged molecule, suggesting splitting of a basic peptide (s). The ϵ-prototoxin and ϵ-toxin show complete immunologic identity." @default.
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- W1483281977 date "1969-01-01" @default.
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- W1483281977 title "Studies on ϵ-prototoxin of Clostridium perfringens type D" @default.
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- W1483281977 doi "https://doi.org/10.1016/0003-9861(69)90055-1" @default.
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