Glutathion s-transferase enzymepurification from the liver of goose (Anser Anser Domesticus),investigation of characterization, effects of somechemicals and metals on enzyme activity

In this thesis, purification and characterization of Glutathione S-transferase (GST; EC 2.5.1.18) enzyme in goose (Anatidae) liver tissue and the effects of some chemicals on enzyme activity were investigated. Affinity chromatography method was used for the purification of GST enzyme from goose liver tissue. With this method, the enzyme was purified 48.4 times with a yield of 70.51.25% with a protein specific activity of 0.121 EU/mg. The purity of the purified enzyme was checked by SDS-polyacrylamide gel electrophoresis and a single band was obtained. The molecular weight has been calculated as approximately 23 kDa. The optimum pH of the enzyme is 7, its stable pH is 6.5, its optimum ionic strength is 100 mM K-phosphate and finally its optimum temperature is calculated as 40 °C. In addition, the KM constant for the GSH substrate was 1.34 mM and the Vmax value was 01.14 EU/ml, the KM constant for the CDNB substrate was 0.68 mM and the Vmax value was 0.5 EU/ml. Finally, the inhibition effects of metal ions such as Se-2, Hg+2, Ag+, and Fe+2 and the chemicals Oxytetracycline, Tylosin Tartrate, Enrofloxacin and Doxycycline on the GST enzyme purified from goose liver tissue were examined and the IC50 values of these chemicals and metal ions were calculated.