Characterization of an enzyme from Phaseolus vulgaris seeds which hydroxylates GAi to GA8 |
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Authors: | Richard Patterson Lawrence Rappaport R.William Breidenbach |
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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. |
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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. |
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Keywords: | Leguminosae snap bean mixed function oxidase hydroxylating enzyme |
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