Purification and Some Properties of Talopeptin (MK-I), a Novel Proteinase Inhibitor Produced by Streptomyces mozunensis MK-23
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概要
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A novel proteinase inhibitor, talopeptin (MK-I), was found in the culture filtrate of Streptomyces mozunensis MK-23, which is a new species of the genus Streptomyces. Talopeptin was successively purified from the culture filtrate by carbon adsorption, butanol extraction, and DEAE-Sephadex A-25, carbon and Sephadex G-10 chromatographies. The structure was elucidated to be 6-deoxy-α-L-talopyranosyloxyphospho-L-leucyl-L-tryptophan as described previously.1) Talopeptin is stable in neutral or alkaline solutions, but unstable in an acidic solution. Inhibitory activity of talopeptin against thermolysin noticeably decreased at pHs higher than 7.
- 社団法人 日本農芸化学会の論文
著者
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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FUKUHARA Ken-ichi
Department of Agricultural Chemistry, University of Osaka Prefecture
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KATSURA Minoru
Department of Agricultural Chemistry, University of Osaka Prefecture
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