Purification to homogeneity of spinach nitrite reductase by ferredoxin-sepharose affinity chromatography.
Assimilatory nitrite reductase was purified 1,700-fold with a yield of 22% from spinach leaves with a procedure involving ammonium sulfate fractionation, DEAE-cellulose and DEAE-Sephadex chromatography, gel filtration and ferredoxin-Sepharose affinity chromatography. The purified enzyme was apparently homogeneous as shown by disc and SDS-gel electrophoresis with a specific activity (mumol NO2-reduced/min/mg protein) of 140.
D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005288:Ferredoxins; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D009572:Nitrite Reductases / Q000302:isolation & purification*; D010944:Plants / Q000201:enzymology; D012685:Sepharose
D005288:Ferredoxins; D012685:Sepharose; D009247:NADH, NADPH Oxidoreductases; D009572:Nitrite Reductases