Abstract
A trypsin-like proteinase was isolated from Streptomyces rimosus culture filtrates obtained from an oxytetracycline production process. The isolation procedure includes ultrafiltration, chromatography on CM-Sephadex, AH-Sepharose and CM-cellulose. Like other streptomycete trypsins, it is a more efficient catalyst than bovine trypsin and has a relative preference for peptide-arylamides, Nα-benzyloxycarbonyl-L-norleucyl-L-propyl-L-arginine-p-nitroanilide being by far its best substrate
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