Akademik Veri Yönetim Sistemi
TURKISH JOURNAL OF VETERINARY & ANIMAL SCIENCES, cilt.36, sa.5, ss.546-553, 2012 (SCI-Expanded)
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, K-i 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.