Isoflavone Synthase from Cell Suspension Cultures of Pueraria lobata
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概要
- 論文の詳細を見る
Liquiritigenin and isoliquiritigenin were converted into daidzein by a microsomal fraction of cell suspension cultures of Pueraria lobata OHWI, which had been treated with an endogenous elicitor prepared by hydrolysis of their own cell walls with a fungal endopolygalacturonase. Competitive experiments with [^3H]flavanone and [^<14>C]chalcone as the substrates for isoflavone synthase revealed that flavanone is the true substrate for this enzyme reaction and the possible role of chalcone in the reaction is excluded.
- 社団法人日本薬学会の論文
- 1990-07-25
著者
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三川 潮
Faculty of Pharmaceutical Sciences, University of Tokyo
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野口 博司
静岡県大薬
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野口 博司
静岡県立大学薬学部
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袴塚 高志
東大薬
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袴塚 高志
Faculty of Pharmaceutical Sciences, The University of Tokyo
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野口 博司
Faculty of Pharmaceutical Sciences, The University of Tokyo
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海老塚 豊
Faculty of Pharmaceutical Sciences, The University of Tokyo
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三川 潮
富山医薬大薬
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三川 潮
Faculty Of Pharmaceuical Sciences The University Of Tokyo
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三川 潮
Faculty Of Pharmaceutical Sciences University Of Tokyo
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三川 潮
東大 薬
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Sankawa U
International Research Center For Traditional Medicine
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Sankawa Ushio
(present Address)faculty Of Pharmaceutical Sciences Toyama Medical And Pharmaceutical University
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Sankawa Ushio
Faculty Of Pharmaceutical Sciences Toyama Medical And Pharmaceutical University
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野口 博司
Faculty Of Pharmaceutical Sciences The University Of Tokyo
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- ISOLATION, SEQUENCE AND BACTERIAL EXPRESSION OF A cDNA FOR CHALCONE SYNTHASE FROM THE CULTURED CELLS OF PUERARIA LOBATA
- Isoflavone Synthase from Cell Suspension Cultures of Pueraria lobata
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