Zaric, YakupYerlikaya, EmrahDemirdag, Ramazan2019-11-182019-11-182019https://hdl.handle.net/20.500.12604/1619Glutathione-S-Transferases (GSTs) are xenobiotic metabolizing enzymes that protect cells from toxic drugs and environmental electrophiles. Furthermore, these enzymes have effected the regulators of oxidative stress and toxicity [1]. In earlier studies; GST enzymes have been purified and characterized from many living things such as sheep, bird, fish, bacterium, bovine and human. This study proves the purification and characterization of GST enzyme (E.C. 2.5.1.18) from the Gill Tissue of Lake Van Fish by affinity chromatography. Inhibitory effects of some metal ions and pesticides on GST activity were determined with using the CDNB method under in vitro conditions. Purification degree for the purified enzyme was controlled by SDS-PAGE. Optimal pH, optimal ionic strength, optimal temperature and stable pH were determined as 7.3, 120 mM, 35°C, 8.0, respectively. Inhibitory effects of Al3+, Ba2+, B3+ and Se2- metal ions and Oxamyl, Diniconazole, Carbofuran, Tebuconazole and Atrazine pesticides have been examined on the purified GST enzyme. Inhibition graphics have been drawn in order to find the IC50 values of metals and pesticides showing inhibition from Activity % -[Inhibitor] graphs. Consequently, in vitro inhibition rank order was determined as Al3+ > Ba2+ > Se2- > B3+ for metal ions, Carbofuran > Tebuconazole > Oxamyl > Atrazine > Diniconazole for pesticides.eninfo:eu-repo/semantics/openAccessAffinity, Metal Ion, Pesticide, Inhibition, GillArticleQ4WOS:000503915900004