The action of proteolytic enzymes on Clostridium botulinum type A toxin

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Abstract
Two forms of crystalline C. botulinum type A toxin were prepared. One of these was low in specific activity ("partially pure") and was highly unstable at pH 7.0, while the 2nd form possessed much higher specific activity ("pure" toxin) and was more stable at pH 7.0. The action of crystalline proteolytic enzymes on the "pure" toxin was investigated. With the conditions adopted, papain had no inactivating effect, pepsin produced slight detoxication while trypsin greatly lowered the toxicity. In none of the enzymic experiments was any toxic product of low molecular weight produced.