Effect of ascorbic acid on the production of singlet oxygen by purified human myeloperoxidase.
We have previously studied purified human myeloperoxidase-hydrogen peroxide-halide ion systems as models of possible singlet oxygen production by granulocytes. While myeloperoxidase could efficiently produce singlet oxygen, the yield of singlet oxygen at a physiological pH with Cl- was very small due to enzyme inactivation. In that Bolscher et al. [(1984) Biochim. Biophys. Acta 784, 189-191] observed that micromolar concentrations of ascorbic acid prevented inactivation of myeloperoxidase and increased the production of hypochlorous acid, we examined whether ascorbic acid would augment singlet oxygen production by the myeloperoxidase-hydrogen peroxide-halide ion systems. Ascorbic acid, however, fails to increase the singlet oxygen yield, suggesting that it does not augment singlet oxygen production in the intact granulocyte by a myeloperoxidase-dependent mechanism.
Kanofsky
J R
JR
Wright
J
J
Tauber
A I
AI
D001205:Ascorbic Acid / Q000494:pharmacology*; D002712:Chlorides / Q000494:pharmacology; D006098:Granulocytes / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000097:blood; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008954:Models, Biological; D010100:Oxygen / Q000097:blood; D009195:Peroxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D026082:Singlet Oxygen
D002712:Chlorides; D026082:Singlet Oxygen; D006861:Hydrogen Peroxide; D010544:Peroxidases; D009195:Peroxidase; D001205:Ascorbic Acid; D010100:Oxygen