Purification and Characterization of a Cysteine Protease from Corms of Freesia, Freesia reflacta
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概要
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A protease (freesia protease B) has been purified to electrophoretic homogeneity from corms of freesia, Freesia reflacta by five steps of chromatography. Its M_r was estimated to be about 26,000 by SDS-PAGE. The optimum pH of the enzyme was 6.0-7.0 at 30℃ using casein as a substrate. The enzyme was strongly inhibited by p-chloromercuribenzoic acid but not by phenylmethanesulphonylfluoride and EDTA. These results indicate that freesia protease B is a cysteine protease. Nine sites of oxidized insulin B-chain were cleaved by freesia protease B in 24 h of hydrolysis. The four cleavage sites among them resembled those of papain. From the digestion of five peptidyl substrates the specificity of freesia protease B was found to be approximately broad, but the preferential cleavage sites were negatively charged residues at P'_1 positions. Freesia protease B preferred also the large hydrophobic amino acid residues at the P_2 position, in a similar manner to papain. The amino terminal sequence of freesia protease B was identical with those of papain in regard to the conservative residues of cysteine protease.
- 社団法人日本農芸化学会の論文
- 1997-09-23
著者
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Kaneda M
Department Of Chemistry Faculty Of Science Kagoshima University
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YONEZAWA Hiroo
Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kagoshima University
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KANEDA Makoto
Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kagoshima University
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UCHIKOBA Tetsuya
Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kagoshima University
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Yonezawa Hiroo
Laboratory Of Biochemistry Department Of Chemistry Faculty Of Science Kagoshima University
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UCHIKOBA Tetsuya
Kagoshima University Musium
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Uchikoba T
Kagoshima University Musium
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Kaneda Makoto
Laboratory Of Animal Breeding And Genetics Graduate School Of Agricultural Science Kobe University
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