Purification and Characterization of Assimilatory Nitrate Reductase from the Cyanobacterium Plectonema boryanum
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概要
- 論文の詳細を見る
Assimilatory nitrate reductase (NR) was solubilized by acetone treatment from Plectonema boryanwn and was purified 7,700-fold by heat treatment, ammonium sulfate fractionation and chromatography on DEAE-Sephacel and Sephadex G-150. Purified NR had a specific activity of 85 ,μmol NO_2^- formed min^<-1> mg^<-1> protein. The enzyme retained both ferredoxin (Fd)- and methyl viologen (MV)-linked NR activities throughout the purification procedure. Molecular weight was 80,000. The pH optimum was 10.5 in the MV-assay and 8.5 when assayed with enzymatically reduced Fd as the electron donor. Apparent Km values for nitrate and MV were 700 μM and 2,500 μM in the MV-assay and 55 μM and 75 μM for nitrate and Fd in the Fd-assay. The enzyme was inhibited by thiol reagents and metal-chelating reagents.
- 日本植物生理学会の論文
著者
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Ida Shoji
The Research Institute for Food Science, Kyoto University
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Ida Shoji
The Research Institute For Food Science Kyoto University
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MIKAMI Bunzo
The Research Institute for Food Science, Kyoto University
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Mikami Bunzo
The Research Institute For Food Science Kyoto University
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