In the course of an intensive screening for inhibitors of aminopeptidase M, a peptide-like inhibitor was isolated from an actinomycete strain, which was identified as Streptomyces sp, SL387. The yield improvement and fermentation studies of this strain were also done for obtaining a sufficient amount of substances for chemical studies and for biological evaluation of inhibitor. This inhibitor was purified by use of column chromatography of Amberlite XAD-2, Dove-ex 50, DEAF-cellulose, MCI gel, Sephadex LH-20, Europrep 60-60 C_(18)(ODS) gel, and then isolated through HPLC as colorless powder. The purified inhibitor was competitive with substrate, and IC_(50) of it was 0.05 §¶/§¢.
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