Presence of cytochrome b−245 in NADPH oxidase preparations from human neutrophils

AbstractThe composition of NADPH oxidase purified by Red Sepharose chromatography of extracts from human neutrophil membranes was investigated. In contrast to that was recently reported by others, the enzyme isolated according to this procedure contained a high concentration of cytochrome b−245 and little FAD. The results reinforce the belief that cytochrome b−245 is a major component of the NADPH oxidase and plays a fundamental role in the formation of O2− by neutrophils