Purification and Characterization of Fe(III)-EDTA Reductase from Bacillus sp. B-3
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概要
- 論文の詳細を見る
Fe(III)-EDTA reductase was purified from Bacillus sp. B-3 isolated as a Fe(III)-EDTA-degrading bacterium. The purified enzyme showed a single protein band corresponding to a molecular mass of 19 kDa on SDS–PAGE, and had FMN as cofactor. It was alkali-thermostable. Its N-terminal amino acid sequence was identical with that of NADPH azoreductase from several species of Bacillus.
- 社団法人 日本農芸化学会の論文
- 2011-10-23
著者
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SHINAGAWA Emiko
Department of Chemical and biological Engineering, Ube National College of Technology
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Shinagawa Emiko
Department Of Chemical And Biological Engineering Ube National College Of Technology
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Shinagawa Emiko
Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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