STUDIES ON PLANT FLAVOKINASE:II. THE PURIFICATION AND SOME PROPERTIES OF BEAN FLAVOKINASE
スポンサーリンク
概要
- 論文の詳細を見る
1. Bean flavokinase has been highly purified to the specific activity of 80 mμmoles FMN formed per hour per mg protein at 30° by protamine treatment, fractionation with ammonium sulfate and chromatography on DEAE-cellulose. This preparation did not contain phosphatase activity and practically behaved as a homogeneous system in electrophoresis and ultracentrifugation.2. The optimum pH was around 9.0 and the optimum temperature for the enzyme activity was abount 40°.3. The metallic ions, especially Mg2+ was essential for full activity of the enzyme.4. ATP was shown to be the specific phosphate donor. While ADP had a slight effect on the phosphorylation, GTP, CTP and ITP were entirely ineffective.5. The enzyme was half saturated with riboflavin at the concentration of 1.3×10-5 M.
- 日本ビタミン学会の論文
著者
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満田 久輝
Laboratory of Nutritional Chemistry, Faculty of Agriculture, Kyoto University
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友沢 靖子
Laboratory of Nutritional Chemistry, Faculty of Agriculture, Kyoto University
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満田 久輝
Laboratory of Nutritional Chemistry, Department of Food Science and Technology, Faculty of Agriculture, Kyoto Univeristy
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河合 文雄
Laboratory of Food Science and Technology, Research Institute for Production Development
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