Respiratory burst oxidase from human neutrophils: purification and some properties.
The respiratory burst oxidase of human neutrophils was purified by "dye-affinity" chromatography over a red agarose column. Electrophoresis of the purified enzyme on NaDodSO4 gel showed a single major band at 64,000-66,000 daltons, together with some minor contaminants. On a nondenaturing gel, the enzyme ran as two closely spaced bands, the faster of which contained flavin. When these two bands were rerun separately on a NaDodSO4 gel, they gave identical patterns, each showing a major band at ca. 65,000 daltons. The specific activity (mean +/- SEM) of the purified enzyme was 8.8 +/- 3.5 mumol of O-2 per min/mg of protein.
D002462:Cell Membrane / Q000201:enzymology; D003573:Cytochrome b Group / Q000032:analysis; D005415:Flavins / Q000032:analysis; D006801:Humans; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D019255:NADPH Oxidases; D009504:Neutrophils / Q000201:enzymology*; D045332:Photosystem II Protein Complex; D013057:Spectrum Analysis
D003573:Cytochrome b Group; D005415:Flavins; D045332:Photosystem II Protein Complex; C019313:cytochrome b559; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases; C022709:superoxide-forming enzyme