Purification of a NADH-ferricyanide reductase from plant microsomal membranes with a zwitterionic detergent.
A microsomal NADH-ferricyanide reductase was purified to homogeneity from potato tubers. A zwitterionic detergent (CHAPS) was used for the extraction of this reductase which is the first to be purified from plant microsomal membranes. The successive steps of purification included an anion exchange column (DEAE-cellulose or DEAE-Trisacryl), a blue-Ultrogel affinity column and a gel filtration on Sephadex G75. The purification factor was 280 and the yield was 1.6%. The protein has an apparent molecular weight of 44,000 +/- 1,000 as estimated from SDS-PAGE. This successful purification opens new perspectives in the study of oleate desaturase of higher plants which is assumed to contain NADH-ferricyanide reductase as an essential component.
D002793:Cholic Acids; D007425:Intracellular Membranes / Q000201:enzymology*; D008861:Microsomes / Q000201:enzymology*; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D013053:Spectrophotometry
D002793:Cholic Acids; D009247:NADH, NADPH Oxidoreductases; C014227:ferricyanide reductase; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate