Purification and characterization of microsomal cytochrome b560ms from a unicellular eukaryote Tetrahymena pyriformis.

摘要: Abstract Effective resolution of detergent-solubilized Tetrahymena microsomal cytochrome b560ms, which is similar to mammalian b5, was obtained by chromatography on DEAE-cellulose and gel filtration. On the basis sodium dodecyl sulfate-polyacrylamide electrophoresis, molecular weight b560ms 22,000. The absorption peaks are 414 nm in oxidized form 560, 528, 425 dithionite-reduced form. alpha-peak reduced form, situated at 560 asymmetric with a shoulder 556 nm, different from that liver b5. spectra not altered presence cyanide, azide, carbon monoxide. resolved into two distinct 551 558 low temperature. 557, 527, 418 pyridine ferrohemochrome spectrum indicate protoheme prosthetic group purified b-type cytochrome. oxidation-reduction potential (E'0) -42 mV. It reducible NADH an NADH-cytochrome b5 reductase rat microsomes. present results suggest pathways electrons b560ms-linked oxidative desaturation fatty acyl-CoA protozoan pyriformis via either flavoprotein reductases, NADH-ferricyanide or NADPH-cytochrome c reductase.