Purification and Properties of a New Enzyme, D-Carnitine Dehydrogenase, from Agrobacterium sp. 525a
スポンサーリンク
概要
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A new enzyme, D-carnitine dehydrogenase from Agrobacterium sp. 525a, was purified by DEAE-Toyopearl, ammonium sulfate fractionation, Sephadex G-75, affinity chromatography, and Mono Q and TSK-gel filtration column chromatography. The enzyme had the molecular mass of 89 kDa and consisted of three identical subunits. The optimum pH for the oxidation reaction was 9.3. The Michaelis constants for D-carnitine and NAD^+ were 3.1 and 0.07 mM, respectively. The N-terminal 20 amino acids were sequenced.
- 社団法人日本農芸化学会の論文
- 1997-06-23
著者
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MORI Nobuhiro
Department of Agricultural, Biological, and Environmental Sciences, Faculty of Agriculture, Tottori
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KITAMOTO Yutaka
Department of Bioscience and Biotechnology, Faculty of Agriculture, Tottori University
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Kitamoto Yutaka
Department Of Agricucultural Chemistry Faculty Of Agriculture Tottori University
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Kitamoto Yutaka
Department Of Biochemistry And Biotechnology Faculty Of Agriculture Tottori University
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SETYAHAD Siswa
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University
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UEYAMA Tomoko
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University
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ARIMOTO Takeshi
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University
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Ueyama Tomoko
Department Of Biochemistry And Biotechnology Faculty Of Agriculture Tottori University
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Setyahad Siswa
Department Of Biochemistry And Biotechnology Faculty Of Agriculture Tottori University
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Mori Nobuhiro
Department Of Agricultural Biological And Environmental Sciences Faculty Of Agriculture Tottori Univ
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Arimoto Takeshi
Department Of Biochemistry And Biotechnology Faculty Of Agriculture Tottori University
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Setyahadi Siswa
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University
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