Isolation and Characterization of Manganese-containing Superoxide Dismutase from Gluconobacter cerinus(Biological Chemistry)
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概要
- 論文の詳細を見る
Among 21 strains of Gluconobacter, Gluconobacter cerinus (IFO 3268) had a thermostable superoxide dismutase activity. The enzyme was purified about 110-fold to homogeneity from a cell -free extract by ammonium sulfate fractionation and DEAE-Toyopearl and Sephadex G-100 chromatography. The enzyme has a molecular weight of 47,000 and consists of two identical subunits, and contains 1.22g atoms of Mn per mole of enzyme as the catalytically active metal. The enzyme disappeared from circulation in the guinea pig with a half-life of 45min, but enzyme modified with polyethylene glycol 5,000 had a half-life of 330min.
- 社団法人日本農芸化学会の論文
- 1987-12-23
著者
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SODA Kenji
Laboratory of Microbiology, Institute for Chemical Research, Kyoto University
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Soda Kenji
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Tsukuda K
Pias Corp. Osaka
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Tsukuda Koji
Research And Development Center Pias Corporation
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Kido Toshiko
Laboratory Of Microbial Biochemistry Institute Of Chemical Research Kyoto University
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SHIMASUE Yoshiyuki
Research and Development Center, Pias Corporation
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UEDA Sueyoshi
Research and Development Center, Pias Corporation
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TERAKAWA Masumi
Research and Development Center, Pias Corporation
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Ueda Sueyoshi
Research And Development Center Pias Corporation
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Shimasue Y
Pias Corp. Osaka
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Shimasue Yoshiyuki
Research And Development Center Pias Corporation
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Terakawa Masumi
Research And Development Center Pias Corporation
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Soda Kenji
Laboratory Of Microbial Biochemistry Institute Of Chemical Research Kyoto University
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