STUDIES ON PLANT FLAVOKINASE

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Abstract
Bean flavokinase was highly purified to the specific activity of 80 m[mu] moles FMN formed per hour per mg protein at 30[degree] 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. The optimum pH was around 9.0 and the optimum temperature for the enzyme activity was about 40[degree]. The metallic ions, especially Mg2+ was essential for full activity of the enzyme. ATP was shown to be the specific phosphate donor. While ADP had a slight effect on the phos-phorylation, GTP, CTP and ITP were entirely ineffective. The enzyme was half saturated with riboflavin at the concentration of 1.3 x 10-5 M.