Purification of glutathione reductase enzyme from scorpion fish (Scorpaena porcus) liver tissue and investigation of some heavy metal inhibition kinetics

In the current syudy, glutathione reductase was purified from Scorpion fish (Scorpaena porcus) liver tissue and the effects of heavy metal ions on the enzyme activity were determined. The purification process consisted of three stages; preparation of the homogenate, ammonium sulfate precipitation and affinity chromatography purification. At the end of these steps, the enzyme was purified 25.9-fold with a specific activity of 10,479 EU/mg and a yield of 28.3 %. The optimum pH was found to be 6.5, optimum substrate concentration was 0.3 mM NADPH and optimum buffer was 300 mM KH2PO4. After purification, inhibition effects of Mn+2, Cd+2 , Ni+2, and Cr+3, as heavy metal ions were investigated. IC50 values of the heavy metals were calculated as 2.4 µM, 30 µM, 135 µM and 206 µM, respectively.