Purification and Some Properties of FMPI, a Novel Metallo-proteinase Inhibitor Produced by Streptomyces rishiriensis NK-122
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概要
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A novel metallo-proteinase inhibitor (FMPI) was purified about 10, 000 times from the culture filtrate of Streptomyces rishiriensis NK-122 through column chromatographies on Dowex 1 × 2 (OH-) form, aluminum oxide, Dowex 1 × 2 (OH-) form, XAD-2, Cellulofine GC-15 and Sephadex LH-20, successively. FMPI was homogeneous on thin-layer and high performance liquid chromatographies. FMPI is composed of L-phenylalanyl-L-arginine and phosphoric acid, its color reaction is positive for Rydon-Smith, Sakaguchi and ammonium molybdate-perchloric acid reagents and negative for ninhydrin, Pauly, Ehrlich, phenol-sulfuric acid, Folin-Ciocalteau and Tollens reagents. FMPI is stable in a strongly alkaline solution (pH > 11) but very labile below pH 11 even at room temperature.
- 社団法人 日本農芸化学会の論文
著者
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Murao Sawao
Laboratory Of Applied Microbiology College Of Agriculture
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MURAO Sawao
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, University of Osaka Prefecture
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KASAI Naoya
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, University of Osaka Prefecture
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FUKUHARA Ken-ichi
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, University of Osaka Prefecture
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