ESR signals from stimulated and resting porcine blood neutrophils.
The NADPH oxidase in neutrophils was specifically solubilized from membrane vesicles of porcine blood neutrophils and rapidly concentrated by immunoprecipitation with cross-reacting anti-P-450 reductase IgG. The precipitates from both myristic acid-stimulated and resting cells contained one third of the cytochrome b-558 and were slightly contaminated with myeloperoxidase. The immunoprecipitate from stimulated cells gave rhombic high-spin ESR signals of a heme at g = 6.47 and 5.49, which were insensitive to KCN, whereas the preparation from resting cells did not give these signals. The rhombic high-spin signals are discussed in view of the participation of cytochrome b-558 in the NADPH oxidase system.
D000818:Animals; D003573:Cytochrome b Group / Q000097:blood; D004578:Electron Spin Resonance Spectroscopy; D019814:Myristic Acid; D009227:Myristic Acids / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000097:blood*; D019255:NADPH Oxidases; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D011190:Potassium Cyanide / Q000494:pharmacology; D013481:Superoxides / Q000097:blood; D013552:Swine
D003573:Cytochrome b Group; D009227:Myristic Acids; D019814:Myristic Acid; D013481:Superoxides; C036888:cytochrome b558; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases; D011190:Potassium Cyanide