Purification and Characterization of a 0-Methyltransferase Capable of Methylating 2-Hydroxy-3-alkylpyrazine from Vitis vinifera L. (cv. Cabernet Sauvignon)(Biochemistry & Molecular Biology)
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概要
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An 5-adenosyl-L-methionine-dependent 0-methyl-transferase capable of methylating 2-hydroxy-3-alkylpyrazine (HP) was purified 7,300-fold to apparent homogeneity with an 8.2% overall recovery from Vitis vinifera L. (cv. Cabernet Sauvignon) through a purification procedure including column chromatography on DEAE-Sepharose FF, Ether-5PW, hydroxyapatite, G2000SWXL, and DEAE-5PW. The relative molecular mass of the native enzyme estimated on gel permeation chromatography was 85 kDa, and the subunit molecular mass was estimated to be 41 kDa on SDS-polyacrylamide gel electrophoresis. The enzyme also methylates caffeic acid. The V_<max> for IBHP and caffeic acid were 0.73 and 175 pkatals/mg, respectively, and the respective K_m for IBHP and caffeic acid were 0.30 and 0.032 mм. The optimum pH for IBHP (8.5) was different from that for caffeic acid (7.5).
- 社団法人日本農芸化学会の論文
- 2001-10-23
著者
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HASHIZUME Katsumi
National Research Institute of Brewing
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HIRAGA Yoshikazu
Department of Chemistry, Graduate School of Science, Hiroshima University
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ARAMAKI ISAO
National Research Institute of Brewing
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TOZAWA Kazuyuki
National Research Institute of Brewing
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Hiraga Yoshikazu
Department Of Chemistry Graduate School Of Science Hiroshima University
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Hiraga Yoshikazu
Department Of Chemistry Facalty Of Science Hiroshima University
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