Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
PubMedPublished 1 July 1967
Donald E. Paglia, William N. Valentine
Citations10,806
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TL;DR
Glutathione peroxidase activity is found to be associated with a relatively stable, nondialyzable, heat-labile, intracellular component which is separable from hemoglobin, by gel filtration and ammonium sulfate precipitation.
Abstract
Abstract An assay procedure is described in which blood cell glutathione peroxidase may be accurately measured by a direct spectrophotometric procedure. Glutathione peroxidase activity is found to be associated with a relatively stable, nondialyzable, heat-labile, intracellular component which is separable from hemoglobin, by gel filtration and ammonium sulfate precipitation. The activity appears to be dependent upon active sulfhydryl groups and is unaffected by low concentrations of azide, cyanide, or ferricyanide.
Keywords
MedicineBiochemistry, Genetics and Molecular BiologyEngineering
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