Activation of Clostridium botulinum type B and E derivative toxins with lysine-specific proteases |
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Authors: | Shunji Kozaki Yasuhiro Oga Yoichi Kamata Genji Sakaguchi |
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Institution: | Department of Veterinary Science, College of Agriculture, University of Osaka Prefecture, Sakai-shi, Osaka 591, Japan |
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Abstract: | Abstract Clostridium botulinum type B and E derivative toxins were activated with lysyl endopeptidase or endoproteinase Lys-C, which splits only the bond involving the carboxyl group of a lysine residue. Type B toxin was more efficiently activated with lysyl endopeptidase; type E toxin was more efficiently activated with trypsin. Type B toxin was split by the lysine-specific protease into 2 fragments of molecular sizes indistinguishable from those induced with trypsin. Type E toxin was split by the same protease into 3 fragments, 2 of which had M r identical to those obtained with trypsin, the other having an M r less than that of the heavy chain but greater than that of the light chain. These results attest that both activation and nicking of type B and E derivative toxins are ascribable to cleavage, not of an arginyl, but of a lysyl bond. |
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Keywords: | Activation nicking lysyl endopeptidase endoproteinase Lys-C Clostridium botulinum type B and type E derivative toxin |
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