Isolation and Characterization of a Cysteine Protease of Freesia Corms(Biochemistry & Molecular Biology)
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概要
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A protease, freesia protease (FP)-A, was purified to electrophoretic homogeneity from regular freesia (Freesia reflactd) corms in harvest time. The M_r of FP-A was estimated to be 24 k by SDS-PAGE. The optimum pH of the enzyme was 8.0 using a casein substrate. These enzymes were strongly inhibited by p-chloromercuribenzoic acid but not by phenylmethane-sulfonylfluoride and EDTA. These results indicate that FP-A belongs to the cysteine proteases. The amino terminal sequence of FP-A was similar to that of papain, and the sequences was regarded to the conservative residues of cysteine protease. From the hydrolysis of peptidyl-p-NAs, the specificity of FP-A was found to be broad. It was thought that FP-A was a new protease from freesia corms.
- 社団法人日本農芸化学会の論文
- 2002-02-23
著者
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YONEZAWA Hiroo
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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Arima Kazunari
Laboratory Of Biochemistry Department Of Chemistry Faculty Of Science Kagoshima University
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Okubo Michiko
Department Of Health And Nutrition Kagoshima Immaculate Heart University
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UCHIKOBA Tetsuya
Kagoshima University Musium
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OKUBO Michiko
Food and Nutrition, Kagoshima Immaculate Heart College
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Uchikoba T
Kagoshima University Musium
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