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 the formation of mercapturic acid, the end product in detoxification metabolism. They can prevent reactive electrophilic compounds from harming the body by covalently binding the same type of compounds to each other. In this study, we determined the in vitro inhibitory effects of metal ions such as Cu 2+ , Cd 2+ , Ag + , and Co 2+ on GST enzyme activity. For this aim, GST was purified from C. tarichi Pallas liver with 37.36% yield and 29.304 EU/mg specific activity using the chromatographic method. The V max values of liver GST were determined for CDNB and GSH to be 1.245 and 0.562 EU/mL, respectively, and the K m values were found 0.89 and 0.06 mM, respectively, using the Lineweaver-Burk plot. The effects of the metal ions at different concentrations on in vitro GST activity were studied. The IC 50 values were determined for Cu +2 , Cd +2 , Ag + , and Co +2 as 0.163, 0.235, 0.00021, and 0.446 mM, respectively. The K i constants were determined as 0.049 ± 0.009, 0.117 ± 0.031, 0.002 ± 0.0007, and 0.893 ± 0.3 mM, respectively. Ag + showed the best inhibitory effect among the studied metal ions. Cd 2+ , Cu 2+ and Co 2+ showed a competitive inhibition mechanism, while Ag + was noncompetitive.