Open AccessActivation of Clostridium botulinum type B and E derivative toxins with lysine‐specific proteases
Author(s) -
Kozaki Shunji,
Oga Yasuhiro,
Kamata Yoichi,
Sakaguchi Genji
Publication year - 1985
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1985.tb00658.x
Subject(s) - trypsin , endopeptidase , clostridium botulinum , lysine , biochemistry , proteases , toxin , protease , chemistry , clostridium , residue (chemistry) , enzyme , biology , amino acid , bacteria , genetics
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.