Abstract
Streptomyces griseoincarnatus strain No. KTo-250 produced three kinds of inhibitors designated as API-2a, b and c. Among them, API-2b was purified previously.1) API-2c, produced rather in late phase of culture, was purified by salting-out with ammonium sulfate, column chromatography on DEAE-cellulose and gel filtration on Sephadex G-100. From the result of amino acid analysis, it was demonstrated that API-2b and c have an isoleucine residue in their molecules. Furthermore, both inhibitors differed from other microbial alkaline protease inhibitors in chemical and physico-chemical properties. API-2b was converted to c by washed mycelium of the strain, and from the examination of the terminal amino acid, some amino acid residues from the amino-terminal part in API-2b are thought to be removed to form API-2c.
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