Purification and Properties of Betaine Aldehyde Dehydrogenase with High Affinity for NADP from Arthrobacter globiformis
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概要
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Betaine aldehyde dehydrogenase from Arthrobacter globiformis was purified to apparent homogeneity by ammonium sulfate fractionation, followed by ion-exchange, butyl-Toyopearl and gel filtration chromatography. The enzyme was found to be a tetramer with identical 55 kDa subunits. Both NAD^+ and NADP^+ could be used as a cofactor for the enzyme and Michaelis constants (K_m value) for NAD^+ and NADP^+ were 1075 μM and 48 μM, respectively. The enzyme was highly specific for betaine aldehyde and the K_m value for betaine aldehyde was 36 μM.
- 社団法人日本生物工学会の論文
- 2002-02-25
著者
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MORI Nobuhiro
Department of Agricultural, Biological, and Environmental Sciences, Faculty of Agriculture, Tottori
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Mori Nobuhiro
Department Of Biochemistry And Biotechnology Faculty Of Agriculture Tottori University
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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 Bioscience And Biotechnology Faculty Of Agriculture Tottori University
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FUCHIGAMI SAYURI
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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Fuchigami Sayuri
Department Of Biochemistry And Biotechnology Faculty Of Agriculture Tottori University
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Mori Nobuhiro
Department of Biochemistry and Biotechnology Faculty of Agriculture, Tottori University
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