Tyropeptins A and B, New Proteasome Inhibitors Produced by Kitasatospora sp. MK993-dF2. I. Taxonomy, Isolation, Physico-chemical Properties and Biological Activities.

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  • I. Taxonomy, Isolation, Physico-chemical Properties and Biological Activities

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Abstract

Tyropeptins A and B, new proteasome inhibitors, were isolated from the culture broth of Kitasatospora sp. MK993-dF2. They were purified using ethyl acetate extraction, silica gel column chromatography, Sephadex LH-20 column chromatography and HPLC. Tyropeptin A inhibited the chymotrypsin-like (ChT-L) and trypsin-like (T-L) activities of 20S proteasome with IC50 values of 0.1μg/ml and 1.5μg/ml respectively, but did not inhibit the peptidylglutamyl-peptide hydrolyzing (PGPH) activity of 20S proteasome at a concentration of 100μg/ml. The inhibitory activities of tyropeptin A were about two times as strong as that of tyropeptin B. Taxonomy of the producing strain is also described.

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