SUMMARY: Two serine proteases in extracts of grown to stationary phase were purified to homogeneity using affinity chromatography on gramicidin S-Sepharose 4B. One enzyme was closely related to, if not identical with, the ‘trypsin-like’ protease II of The other was capable of cleaving the subtilisin chromogenic substrate -carbobenzoxy--alanyl--alanyl--leucine--nitroanilide and resembled the intracellular serine proteases of spp. The amino acid composition of this protease was similar to that of the enzyme. These data indicate a relationship between proteolytic enzymes of evolutionary distant Gram-negative Enterobacteriaceae and Gram-positive spore-forming


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