Activation of Clostridium botulinum type E progenitor toxin by twoproteolytic enzymes (proteinases I and II) from Clostridium botulinumtype A.

Abstract

Two proteinases (I & II) were obtained from Clostridium botulinum type A. Progenitor toxin was obtained from Clostridium botulinum type E (non-proteolytic). The toxicity of progenitor toxin was not enhanced by the treatment with these proteinases at pH 7.0 for 24 hr at 37 C. Results presented here failed to confirm the claim of DasGupta et al^<(l)> that an endogenous enzyme obtained from Clostridium botulinum type B activate the progenitor toxin obtained from the same culture medium. Recently. DasGupta et al^<(1)> reported that an endogenous enzyme was released from C. botulinum type B and it was activated the progenitor toxin produced by C. botulinum type B. In order to elucidate the activation of progenitor toxin by proteolytic enzyme (endogenous), we have attempted the purification of progenitor toxin type E (non-proteolytic) and of two proteinases (type A). It was hoped that the mechanism of the activation could be elucidated with the purified materials. In further purification of proteolytic enzyme (crude proteinase) from C. botulinum type A, we were able to separate two proteolytic enzymes (proteinases I and II)^<(2)>. By using the method of sakaguchi et al^<(3)>, we get purified progenitor toxin from C. bolulinum type E (non-proteolytic). This presents evidence of activation of purified progenitor toxin by purified proteolytic enzymes (proteinases I and II).