Abstract
We assessed the reactivity of Sb(V) in human blood. Sb(V) reactivity was determined using an HPLC-HG-AFS hyphenated system. Sb(V) was partially reduced to Sb(III) in blood incubation experiments; however, Sb(III) was a highly unstable species. The addition of 0.1 mol L(-1) EDTA prevented Sb(III) oxidation, thus enabling the detection of the reduction of Sb(V) to Sb(III). The transformation of Sb(V) to Sb(III) in human whole blood was assessed because the reduction of Sb(V) in human blood may likely generate redox side effects. Our results indicate that glutathione was the reducing agent in this reaction and that Sb(V) significantly decreased the GSH/GSSG ratio from 0.32 ± 0.09 to 0.07 ± 0.03. Moreover, the presence of 200 ng mL(-1) of Sb(V) increased the activity of superoxide dismutase from 4.4 ± 0.1 to 7.0 ± 0.4 U mL(-1) and decreased the activity of glutathione peroxidase from 62 ± 1 to 34 ± 2 nmol min(-1) mL(-1).