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