| Literature DB >> 24470246 |
Abstract
Ferredoxin-NADP(+) oxidoreductase from the cyanobacterium Nostoc strain MAC was separated into two fractions by ion-exchange chromatography. Both were purified to electrophoretic homogeneity and exhibited diaphorase and ferredoxin-dependent cytochrome c reductase activity. The activities with three different electron carriers in this latter assay were similar for the two fractions, as were the pH optima in both assays. Each fraction, however, could be resolved into several active components by isoelectric focusing, both after initial separation and following apparent purification by gel filtration on Sephadex G-150, further chromatography on DEAE-cellulose, and use of hydroxylapatite columns.Entities:
Year: 1981 PMID: 24470246 DOI: 10.1007/BF00056264
Source DB: PubMed Journal: Photosynth Res ISSN: 0166-8595 Impact factor: 3.573