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Effect of ascorbic acid on the production of singlet oxygen by purified human myeloperoxidase
Author(s) -
Kanofsky Jeffrey R.,
Wright Jonathan,
Tauber Alfred I.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81263-1
Subject(s) - singlet oxygen , ascorbic acid , myeloperoxidase , chemistry , hydrogen peroxide , hypochlorous acid , oxygen , photochemistry , yield (engineering) , biochemistry , organic chemistry , immunology , biology , materials science , food science , metallurgy , inflammation
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.