A validated method to assess glutathione peroxidase enzyme activity

This article presents a reliable, effective and easy procedure for measuring glutathione peroxidase (Gpx) activity. Enzyme samples were incubated with phosphate buffer, which included the appropriate concentrations of (GSH) peroxide as substrates, to determine Gpx In CUPRAC method, reagent Cu(Nc)22+ was added stop enzymatic reaction after sufficient period incubation. The unreacted substrates acted reduce Cu(II)–neocuproine complex into strongly coloured Cu(I)–neocuproine that could be measured spectrophotometrically at 450 nm. GPx activity linked decrease in absorbance complex. Box–Behnken design used optimise formation Response surface methodology applied accuracy method. new protocol confirmed by performing Bland–Altman plot analysis matched through Gpx–DTNB assay. correlation coefficient between two protocols 0.9967. result indicated very accurate on par comparison