produced an extracellular SDS-resistant protease (protease A) with an apparent of approximately 54000 when cultured in complex, proteinaceous media. Ca 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 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 -phenanthroline, quinacrine and lack of aeration.


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