Extraction and Affinity Purification of NADH : Nitrate Reductase from Barley (Hordeum distichum L.) Roots
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概要
- 論文の詳細を見る
Conditions suited for the extraction and purification of NADH:nitrate reductase (NR) from barley (Hordeum distichum L.) roots were examined. The addition of 10 mM EDTA to the extraction medium produced an 8-fold increase in the NR activity in the crude extract, whereas the presence of cysteine in the medium caused an appreciable decrease in this activity. EDTA and FAD stimulated NR activity in the crude extract; cysteine inhibited it. The effect of EDTA seemed to be due to the inhibition of the contaminating NADH-oxidizing system. The NADH:NR was purified 300-fold by ammonium sulfate fractionation and blue dextran-Sepharose affinity chromatography. The specific activity was 1,420 nmol nitrite formed min^<-1> mg protein^<-1> at 30℃; the highest specific activity among the NR preparations obtained thus far from root tissues of higher plants. EDTA, as well as cysteine behaved as an inhibitor for the purified NR.
- 日本植物生理学会の論文
著者
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OJI Yoshikiyo
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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Oji Yoshikiyo
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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Miki Yutaka
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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Okamoto Saburo
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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Okamoto Saburo
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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Miki Yutaka
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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