Arylsulfatase from Streptomyces griseorubiginosus S980-14
スポンサーリンク
概要
- 論文の詳細を見る
A new arylsulfatase designated Es-1, which desulfated etoposide 4'-sulfate and p-nitrophenyl sulfate, was isolated from Streptomyces griseorubiginosus S980-14 and purified to protein homogeneity by ammonium sulfate fractionation, ion exchange column chromatography, and chromatofocusing. The enzyme was active in monomeric form with an approximate molecular weight of 45,000, had a pI value of 4.95, and required calcium for full activity. At an optimum reacion pH of 8.5, iodoacetate, mercurous chloride, and EDTA severely inhibited the activity of Es-1 arylsulfatase.
- 社団法人日本農芸化学会の論文
- 1995-06-23
著者
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Sawada Y
Dept. Of Appl. Biol. Sci. Nihon University:(present Office)riken Psc
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Ueki Tomokazu
Bristol-Myers Squibb Research Institute
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Sawada Yosuke
Bristol-Myers Squibb Research Institute
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Fukagawa Yasuo
Bristol-Myers Squibb Research Institute
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Oki Toshikazu
Bristol-Myers Squibb Research Institute
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Oki Toshikazu
Bristol-myers Squibb Research Institute Ltd. Tokyo Research Center
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Fukagawa Yasuo
Bristol-myers Squibb Research Institute Ltd. Tokyo Research Center
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Fukagawa Yasuo
Central Research Laboratories Sanraku Incorporated
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Sawada Y
Bristol-myers Squibb Research Institute:funakoshi Co. Ltd. Life Science Products Division
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