Turkish Journal of Veterinary & Animal Sciences




This study aimed to purify glutathione reductase (GR) from turkey liver and investigate some of its characteristic features. The purification procedure comprised 2 steps: homogenate preparation and 2',5'-ADP Sepharose 4B affinity gel chromatography. Thanks to the 2 consecutive procedures, the enzyme, having the specific activity of 606.67 EU mg protein^{-1}, was purified with a yield of 10.75% and 2476-fold, and, in order to control enzyme purity, SDS-PAGE was done. Optimal pH, stable pH, optimal temperature, optimal ionic strength, molecular weight, turnover number of enzyme, and k_{cat}/K_M and K_M and V_{max} values for NADPH and glutathione disulfide substrates were also determined for the enzyme. In addition, Ki constants and the type of inhibition were determined by means of Lineweaver-Burk graphs obtained for such inhibitors as NADP+ and glutathione. In conclusion, glutathione reductase enzyme was isolated and characterized from turkey liver for the first time, and some of its kinetic properties were determined.

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