Purification and Properties of Betaine Aldehyde Dehydrogenase from Xanthomonas translucens
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概要
- 論文の詳細を見る
Betaine aldehyde dehydrogenase from Xanthomonas translucens was purified to apparent homogeneity by ammonium sulfate fractionation, followed by ion-exchange, butyl-Toyopearl and gel filtration chromatography. The amino acid composition and the N-terminal sequence of 35 amino acid residues were determined. The enzyme was found to be a tetramer with identical 50 kDa subunits. Both NAD and NADP could be used as a cofactor for the enzyme and K_m values for NAD and NADP were 70 μM and 50 μM, respectively. The enzyme was highly specific for betaine aldehyde and the K_m value for betaine aldehyde was 0.19 mM.
- 社団法人日本生物工学会の論文
- 1992-05-25
著者
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MORI Nobuhiro
Department of Agricultural, Biological, and Environmental Sciences, Faculty of Agriculture, Tottori
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Yoshida Naoto
Department Of Biochemistry And Applied Biosciences Faculty Of Agriculture Miyazaki University
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YOSHIDA Nobuyuki
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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Mori Nobuhiro
Department Of Agricultural 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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Kitamoto Yutaka
Department Of Agricucultural Chemistry Faculty Of Agriculture Tottori University
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Yoshida N
Department Of Biochemistry And Applied Biosciences Faculty Of Agriculture Miyazaki University
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Mori Nobuhiro
Department Of Agricultural Biological And Environmental Sciences Faculty Of Agriculture Tottori Univ
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