1. Inhibition of hemoglobin-catalysed glutathione peroxidation and actual values of glutathione peroxidase (E.C.1.11.1.9.) activity in hereditary deficiency of this enzyme
- Author
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A. L. Pawlak
- Subjects
Adult ,Heterozygote ,Erythrocytes ,GPX3 ,Glutathione reductase ,GPX4 ,Hemolysis ,Catalysis ,Hemoglobins ,chemistry.chemical_compound ,Drug Discovery ,Humans ,Genetics (clinical) ,chemistry.chemical_classification ,Carbon Monoxide ,biology ,Chemistry ,Glutathione peroxidase ,Hydrogen Peroxide ,General Medicine ,Glutathione ,Enzyme assay ,Kinetics ,Peroxidases ,Biochemistry ,biology.protein ,Molecular Medicine ,Hemoglobin ,Metabolism, Inborn Errors ,Peroxidase - Abstract
In hemolysates of human red blood cells the reversible inhibition of glutathione peroxidation by hydrogen peroxide has been observed in the presence of HbCO. At 50% HbCO concentration the rate of oxidation was 70% of the normal. At 100% HbCO or CNMetHb the rate of oxidation corresponded to respectively 34% and 37.2% of the normal rate in HbO2 containing hemolysates. It is assumed that at 0.3 mM H2O2 and 0.35 mM Hb (Fe) concentrations the peroxidation of GSH by either HbCO or CNMetHb is negligible as compared to glutatione peroxidase (E.C.1.11.1.9) activity. The peroxidation of GSH in these conditions may be considered as a measure of this enzyme activity. This is supported by studies of glutathione peroxidation in heterzcygotes of glutathione peroxidase deficiency (50% of the normal GSH-px activity in rbc). The previous data on this enzyme defect are reevaluated. more...
- Published
- 1974
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