Activation of Clostridium botulinum type B toxin by an endogenous enzyme.
It was previously postulated, based on indirect evidence, that Clostridium botulinum type B produces neurotoxin which is initially of low toxicity but which then becomes activated to highly toxic form by the action of an endogenous enzyme(s). The first direct in vitro experimental evidence in support of this hypothesis is presented here. The mildly active toxin (progenitor toxin) produced by C. botulinum type B (Lamanna) was isolated from the filtrate of a 24-hr culture and partially purified chromatographically. An enzyme that activates the progenitor toxin was also isolated from the filtrate of a 96-hr culture and purified 200-fold. The enzyme hydrolyzes synthetic substrates of trypsin but not of chymotrypsin.
D000645:Ammonium Sulfate; D000818:Animals; D001905:Botulinum Toxins / Q000302:isolation & purification / Q000633:toxicity*; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003014:Clostridium botulinum / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D003470:Culture Media; D005374:Filtration; D006863:Hydrogen-Ion Concentration; D007275:Injections, Intravenous; D051379:Mice; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D012703:Serotyping; D014357:Trypsin
D003470:Culture Media; D010447:Peptide Hydrolases; D014357:Trypsin; D001905:Botulinum Toxins; D000645:Ammonium Sulfate