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Multiple forms of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase from spinach

1976; Elsevier BV; Volume: 174; Issue: 2 Linguagem: Inglês

10.1016/0003-9861(76)90397-0

1096-0384

Walter W. Fredricks, Judith M. Gehl,

Plant Stress Responses and Tolerance

Crude extracts of ferredoxin-NADP reductase prepared from spinach by three different methods consistently contained two molecular weight forms of the enzyme: P-1, 117,500, and P-2, 50,000. The lower molecular weight form was purified and shown to consist of two different ionic forms. These three forms of the flavoprotein are immunologically identical. A third molecular weight form of the reductase, excluded by Sephadex G-100, generated P-1 and P-2 on rechromatography. Other experiments demonstrated that this enzyme has NADPH-tetrazolium reductase activity and it accounts for essentially all of the tetrazolium reductase activity of isolated chloroplasts.