Isoenzymes of ferredoxin-NADBΔ oxidoreductase from the cyanobacterium Nostoc strain MAC.
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.
Department of Biochemistry, University College of Wales, SY23 3DD, Aberystwyth, Dyfed, Wales, UK.
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GN
Hutber
L J
LJ
Rogers