An EPR study of myeloperoxidase in human granulocytes.
1. EPR spectra of human granulocytes (4 - 10(8) cells per ml) show an intense high-spin ferric heme signal with rhombic symmetry (gx = 6.90 and gy = 5.07) for the heme group. These g-values are identical to those of partially purified myeloperoxidase and thus the signal is derived from ferric myeloperoxidase. In chicken granulocytes, which contain little or no myeloperoxidase, only an axial type of heme iron signal, weak in intensity, can be detected at g = 6.0. 2. Upon phagocytosis of latex particles by human granulocytes the high-spin heme signal with rhombic symmetry is slowly converted into a signal with axial symmetry (gx = gy = 6.0), showing that the EPR signals of myeloperoxidase in the intact cell can be used to study the involvement of the enzyme in metabolic changes during phagocytosis.
D000818:Animals; D002645:Chickens; D004578:Electron Spin Resonance Spectroscopy; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D009195:Peroxidase / Q000097:blood; D010544:Peroxidases / Q000097:blood; D011487:Protein Conformation; D013045:Species Specificity
D010544:Peroxidases; D009195:Peroxidase