| Literature DB >> 914814 |
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.Entities:
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Year: 1977 PMID： 914814 DOI： 10.1093/oxfordjournals.jbchem.a131769
Source DB: PubMed Journal: J Biochem ISSN： 0021-924X Impact factor: 3.387