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Characterization of an enzyme from Phaseolus vulgaris seeds which hydroxylates GAi to GA8
Authors:Richard Patterson  Lawrence Rappaport  R.William Breidenbach
Affiliation:Department of Vegetable Crops, University of California, Davis, CA 95616, U.S.A.;Department of Agronomy, University of California, Davis, CA 95616, U.S.A.
Abstract:Hydroxylation of gibberellin-[3H] A1 (GA1-[3H]) to GA8-[3H] by the 95000 g supernatant fluid from imbibed bean seeds required Fe2+ or Fe3+ and O2 but was insensitive to CO. The hydroxylating enzyme has a sedimentation coefficient of 4·5 S, and was precipitated by (NH4)2SO4 at 35–60% saturation. This hydroxylase was specific for GA1 and did not hydroxylate either pseudo-GA1-[3H] or 16-ketoGA1-[3H]. Virtually all hydroxylase activity was localized in the cotyledons.
Keywords:Leguminosae  snap bean  mixed function oxidase  hydroxylating enzyme
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