{'fraction_non_alphanumeric': 0.027083333333333334, 'fraction_numerical': 0.016666666666666666, 'mean_word_length': 5.449664429530201, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Production and Activation of an SDS-resistant Alkaline Serine Exoprotease of Vibrio alginolyticus

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.