Purification and Some Properties of FMPI, a Novel Metallo-proteinase Inhibitor Produced by Streptomyces rishiriensis NK-122

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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.