PARTIAL PURIFICATION AND SOME PROPERTIES OF EMODIN-O-METHYLTRANSFERASE FROM (+)-GEODIN PRODUCING STRAIN OF ASPERGILLUS TERREUS
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概要
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Emodin-1-O-methyltransferase (E-OMT), an enzyme catalysing methylation of emodin and involved in the biosynthesis of (+)-geodin, was purified upto 89 folds by two-step purification with Blue Sepharose and Sepharose 6B column chromatography. The molecular weight of E-OMT was estimated to be 3.4×10^5,and Km values for emodin and S-adenosylmethionine (SAM) were 3.3×10^<-7>M and 3.1×10^<-6>M, respectively. Substrate specificity of E-OMT was extremely strict, and the enzyme seems to recognize whole the molecule of substrates.
- 公益社団法人日本薬学会の論文
- 1982-06-25
著者
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藤井 勲
岩手医大薬
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三川 潮
Faculty of Pharmaceutical Sciences, 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
Faculty Of Pharmaceuical Sciences The University Of Tokyo
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藤井 勲
東大院・薬
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藤井 勲
Faculty of Pharmaceutical Sciences, University of Tokyo
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