Purification to Homogeneity of Spinach Nitrite Reductase by Ferredoxin-Sepharose Affinity Chromatography
- 1 September 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 82 (3) , 915-918
- https://doi.org/10.1093/oxfordjournals.jbchem.a131769
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 (μmol NO2-reduced/min/mg protein) of 140.This publication has 1 reference indexed in Scilit:
- Chemical Fixation of Enzymes to Cyanogen Halide Activated Polysaccharide CarriersEuropean Journal of Biochemistry, 1971