Oxidation of glutathione by the myeloperoxidase system.
Copyright policy )Oxidation of glutathione by the myeloperoxidase system.
Oxidation of glutathione (GSH) by the myeloperoxidase (MPO) system was studied. The combination of MPO, H2O2, and a halide ion oxidized GSH. This occurred at a H2O2 concentration too low to oxidize GSH by itself. The MPO-mediated oxidation of GSH required the simultaneous presence of MPO, H2O2, and a halide ion. The system had an acid pH optimum of pH 5.5-6.0. Iodide was more effective than bromide which in turn was more effective than chloride. The oxidative product was shown to be GSSG, since it could be reduced back to GSH by glutathione reductase and NADPH. The MPO-mediated oxidation of GSH may be one mechanism by which this system damages microorganisms.
Peroxidases, Neutrophils, Humans, Hydrogen Peroxide, Hydrogen-Ion Concentration, Glutathione, Oxidation-Reduction, Peroxidase
Peroxidases, Neutrophils, Humans, Hydrogen Peroxide, Hydrogen-Ion Concentration, Glutathione, Oxidation-Reduction, Peroxidase
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).14 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!