Purification and Structure of a Novel Cysteine Proteinase Inhibitor, Strepin P-1
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概要
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Strepin P-1, a new proteinase inhibitor, is a low molecular weight peptide isolated from the culture fluid of Streptomyces tanabeensis (SAB-934). Strepin P-1 strongly inhibited not only cysteine proteinases, calpain and papain, but also trypsin. The purification procedures included HP-20 adsorption chromatography, DEAE-cellulose, Amberlite CG-50, Sephadex LH-20 and G-25 column chromatography. The yield was 12mg from 8 liters of culture fluid. The proteinase inhibitor thus prepared was a peptide composed of tyrosine, valine and argininal, that reacted positively with Sakaguchi and Pauly reagents on TLC. The N-terminal amino acid, tyrosine, was blocked with an isovaleryl group and the structure was elucidated to be N-isovaleryl-tyrosyl-valyl-argininal. The amino acid sequence-inhibitory activity relationships of Strepin P-1, leupeptin and antipain toward calpain and papain are also discussed.
著者
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Nomoto Kyosuke
Suntory Institute For Bioorganic Reseach
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TANAKA Takaharu
Laboratory of Biochemistry, Laboratories of Applied Microbiology, Suntory Research Center
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Murachi Takashi
Department Of Clinical Science Faculty Of Medicine Kyoto University
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NAGAI Masami
Laboratory of Applied Microbiology, Research Center, Suntory Ltd.
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OGURA Kyoichi
Laboratory of Applied Microbiology, Research Center, Suntory Ltd.
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MAEDA Mitsuru
Laboratory of Applied Microbiology, Research Center, Suntory Ltd.
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TANAKA Takaharu
Laboratory of Applied Microbiology, Research Center
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