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. 1977 Sep;82(3):915-8.
doi: 10.1093/oxfordjournals.jbchem.a131769.

Purification to homogeneity of spinach nitrite reductase by ferredoxin-sepharose affinity chromatography

S Ida
Free article

Purification to homogeneity of spinach nitrite reductase by ferredoxin-sepharose affinity chromatography

S Ida. J Biochem. 1977 Sep.
Free article

Abstract

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.

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