Spectrophotometric studies on NAD(P)H oxidase of leukocytes. 1. The relationship between granule-NAD(P)H oxidase and myeloperoxidase.
The NAD(P)H oxidase located in granules from resting leukocytes seems to be identical with myeloperoxidase on the basis of the following results. Spectral changes representing the difference between granules with and without NAD(P)H under various conditions represented the formation of compound III of myeloperoxidase, corresponding to the oxidation of NAD(P)H. The KCN difference spectrum of granules from both resting and phagocytizing leukocytes was in agreement with the KCN difference spectrum of myeloperoxidase. The affinity of KCN for myeloperoxidase was the same in both resting and phagocytizing leukocytes. The KCN-sensitive portion of NAD(P)H oxidase of granules from phagocytizing leukocytes seems to be identical with isolated myeloperoxidase and the myeloperoxidase of resting leukocytes. The KCN-insensitive oxidation of NAD(P)H by granules from phagocytizing leukocytes has not been found to be identical with myeloperoxidase.
D000818:Animals; D003486:Cyanides / Q000494:pharmacology; D003594:Cytoplasmic Granules / Q000201:enzymology; D006168:Guinea Pigs; D009247:NADH, NADPH Oxidoreductases / Q000097:blood*; D009504:Neutrophils / Q000201:enzymology*; D009195:Peroxidase / Q000097:blood*; D010544:Peroxidases / Q000097:blood*; D013053:Spectrophotometry
D003486:Cyanides; D010544:Peroxidases; D009195:Peroxidase; D009247:NADH, NADPH Oxidoreductases