PURIFICATION AND CHARACTERIZATION OF DIHYDROGEODIN OXIDASE FROM A FUNGAL STRAIN OF ASPERGILLUS TERREUS PRODUCING (+)-GEODIN
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概要
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Dihydrogeodin oxidase (DHGO), an enzyme catalyzing regio- and stereo-specific intramolecular phenol oxidative coupling reaction of dihydrogeodin to give (+)-geodin, was purified up to homogeneity. DHGO was shown to be a blue copper protein with an absorption maximum at 600 nm. The presence of copper atoms was confirmed by atomic absorption analysis. A molecular weight of 153,000 was estimated for the oxidase and it was composed of two equal molecular weight subunits. DHGO had no phenolase activity and showed strict substrate specificity.
- 公益社団法人日本薬学会の論文
- 1983-01-25
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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飯島 洋
Faculty Of Pharmaceutical Sciences University Of Tokyo
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飯島 洋
キリンビール(株)基盤技術研究所
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飯島 洋
日本大学
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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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