title: ESR signals from stimulated and resting porcine blood neutrophils.
abstract: 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.
mesh_terms: 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
chemical_list: 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