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- W65783484 abstract "Tryptic activation of Clostridium botulinum type E progenitor toxin of 147,000 mol. wt. involves cleavage of the molecule into at least two polypeptides that are separable when the disulfide bond(s) linking them is reduced. The 50,000 and 102,000 mol. wt. of these chains compare with the 53,000 and 97,000 values of the disulfide-linked polypeptides of type A toxin of mol. wt. 145,000. Type E toxin resulting from trypsinization of its progenitor and naturally activated type A and B toxins have similar subunit structures." @default.
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- W65783484 date "1972-07-01" @default.
- W65783484 modified "2023-10-12" @default.
- W65783484 title "A common subunit structure in Clostridium botulinum type A, B and E toxins" @default.
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- W65783484 doi "https://doi.org/10.1016/0006-291x(72)90350-6" @default.
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