Production of Completely Flavinylated Histamine Dehydrogenase, Unique Covalently Bound Flavin, and Iron-Sulfur Cluster-Containing Enzyme of Nocardioides simplex in Escherichia coli, and Its Properties
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概要
- 論文の詳細を見る
The hmd gene of histamine dehydrogenase from Nocardioides simplex was overexpressed in Escherichia coli, and the resulting enzyme was purified to homogeneity. The purified recombinant enzyme is almost identical with the native enzyme in view of molecular weight and specific activity, and is stoichiometrically assembled with the three cofactors 6-S-cysteinyl FMN, 4Fe–4S cluster, and ADP.
- 社団法人 日本農芸化学会の論文
- 2005-12-23
著者
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KANO Kenji
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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IKEDA Tokuji
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Kano Kenji
Kyoto Univ. Kyoto Jpn
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Kano Kenji
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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Ikeda Tokuji
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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FUJIEDA Nobutaka
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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TSUSE Noriaki
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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SATOH Atsuko
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Satoh Atsuko
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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Tsuse Noriaki
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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Kano Kenji
Div. Of Applied Life Sciences Graduate School Of Agriculture Kyoto Univ.
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Kano Kenji
Division Of Applied Life Science Graduate School Of Agriculture Kyoto University
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Fujieda Nobutaka
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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