title: Biological variability of superoxide dismutase and glutathione peroxidase in blood.
abstract: The enzymatic antioxidant defences of mammalian cells include copper-zinc superoxide dismutase (SOD)(Cu Zn-SOD; EC 1.15.1.1) which catalyses the dismutation of superoxide anions (O2(.-)) to hydrogen peroxide(H(2), O(2))and a seleno-dependent glutathione peroxidase (GSH-px) (GSH-px; EC 1.11.1.9) which catalyses the degradation of H(2)O(2) to H(2)O and O(2). The measurement of these enzyme activities is often used as a possible biological index of oxidative stress in various clinical conditions. Complete understanding of such information requires knowledge of the random biological fluctuation of the enzyme activity which occurs in each individual. In the present investigation we examined this normal variability in 12 healthy volunteers (four women and eight men) aged 23-45 years, over 6 months. The intra-individual coefficients of variation (estimated using analysis of variance techniques) were 15% (SOD) and 13% (GSH-px). The analytical goal for imprecision was achieved for both enzymes, i.e. it was less than one half of the measured intra-individual variation. Both enzymes showed marked individuality, indicating that an individual's reference values are more useful than population-based data. The critical difference required for significant changes in serial results is 45% for SOD and 40% for GSH-px.
authors.affiliation: a Department of Clinical Chemistry , The Prince of Wales/Prince Henry Hospitals , Randwick , N.S.W. Australia.
authors.forename: O
authors.initials: O
authors.lastname: Lux
authors.affiliation: a Department of Clinical Chemistry , The Prince of Wales/Prince Henry Hospitals , Randwick , N.S.W. Australia.
authors.forename: D
authors.initials: D
authors.lastname: Naidoo