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Vibrio alginolyticus produced an extracellular SDS-resistant protease (protease A) with an apparent M r of approximately 54000 when cultured in complex, proteinaceous media. Ca2+ was required for the activation and stability of this protease. Its activity was inhibited by EDTA and a serine protease inhibitor, but was not affected by an inhibitor of trypsin-like enzymes. Optimum protease activity occurred under alkaline conditions. Two SDS-resistant exoproteases, B and C, with apparent M r values of approximately 41000 and 37000 respectively, were also produced in complex proteinaceous media. Dialysis of cell-free supernatant samples, which contained predominantly protease A, against distilled water, resulted in increased B and C activity. Production of protease A, B and C activities was inhibited by o-phenanthroline, quinacrine and lack of aeration.
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