Purification and Properties of Sulfite Reductase from Desulfovibrio vulgaris, Miyazaki F

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概要

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• The sulfite reductase of Desulfovibrio vulgaris, strain Miyazaki F (MF), was purified by ammonium sulfate precipitation and chromatography on DEAE-cellulose, Ultrogel AcA34, and hydroxylapatite. The molecular weight was estimated to be 180, 000 by gel filtration. It had a subunit structure of α2β2; the molecular weight of the α subunit was 50, 000 and that of β, 39, 000. The absorption spectrum with characteristic peaks at 629 and 409 nm and the amino acid composition resembled those of the sulfite reductase from D. vulgaris, Miyazaki K. The MF enzyme reduced sulfite to trithionate, thiosulfate, and sulfide by hydrogen when coupled with a hy-drogenase-methyl viologen system, like other sulfite reductases from Desulfovibrio.

• 社団法人 日本農芸化学会の論文

著者

• ISHIMOTO MAKOTO

  Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University

• Ishimoto Makoto

  Department Of Chemical Microbiology Faculty Of Pharmaceutical Sciences Hokkaido University

• AKETAGAWA Jun

  Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University

• KOJO Kimiko

  Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University

関連論文

• CATALYTIC ACTIVITY OF SIROHEME IN REDUCTION REACTION
• Purification and Properties of Sulfite Reductase from Desulfovibrio vulgaris, Miyazaki F

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