Purification and characterization of a protease produced by Vibrio mimicus.

摘要: A protease produced by Vibrio mimicus was purified to apparent homogeneity ammonium sulfate fractionation and successive column chromatography on Sephacryl S-100 Mono Q Monobeads. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) of the final preparation enzyme revealed enzyme. Conventional PAGE showed that migrated as a single band with activity. molecular weight estimated be about 31,000 basis its mobility sulfate-PAGE. had both proteolytic hemagglutination (HA) activities. HA activities were inhibited metalloprotease inhibitors heat treatment. V. therefore appeared heat-labile, bifunctional molecule capable mediating proteolysis HA. immunodiffusion analysis proteases cholerae are immunologically cross-reactive.