Abstract
A SH-dependent protease (SHP) was purified from a culture of C. botulinum type F. The enzyme can activate type E progenitor toxin completely but type B progenitor toxin only partially. SHP by itself probably could completely activate the toxin of proteolytic C. botulinum types A and F in culture. The toxicity of type E progenitor toxin potentiated by the treatment with SHP persisted, but that of derivative toxin decreased rapidly by further incubation with SHP. Apparently, only the progenitor toxin, the complex of the toxic and nontoxic components, activated by SHP withstands the subsequent exposure to the enzyme in cultures of proteolytic C. botulinum.

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