Impacts of some metal ions on glutathione s-transferase in the liver of Chalcalburnus tarichi: an endemic species of Lake Van

Glutathione-S-transferase (GSTs) is a multifunctional enzyme that provides homeostasis by catalyzing the first step of formation mercapturic acid, end product in detoxification metabolism. They can prevent reactive electrophilic compounds from harming body covalently binding same type to each other. In this study, we determined vitro inhibitory effects metal ions such as Cu2+, Cd2+, Ag+, and Co2+ on GST activity. For aim, was purified C. tarichi Pallas liver with 37.36% yield 29.304 EU/mg specific activity using chromatographic method. The Vmax values were for CDNB GSH be 1.245 0.562 EU/mL, respectively, Km found 0.89 0.06 mM, Lineweaver?Burk plot. at different concentrations studied. IC50 Cu+2, Cd+2, Co+2 0.163, 0.235, 0.00021, 0.446 respectively. Ki constants 0.049 ± 0.009, 0.117 0.031, 0.002 0.0007, 0.893 0.3 Ag+ showed best effect among studied ions. Cu2+ competitive inhibition mechanism, while noncompetitive.