Purification and Characterization of Glutathione Reductase Enzyme from Arum Maculatum Leaf

Arum species grow in temperate and Mediterranean climates have been used for hundreds of years food medicinal purposes, although they are highly toxic if not cooked using proper techniques. Glutathione reductase (GR) is a member the pyridine nucleotide disulfide oxidoreductase family flavoenzymes that catalyzes reduction glutathione (GSSG) to reduced GSH NADPH or NADH. In this study, GR enzyme was characterized by partial purification processes including homogenate preparation, ammonium sulfate precipitation dialysis from leaf maculatum plant. The highest activity found at 40-60% saturation range. Optimum ionic strength, pH substrate concentration were investigated A. leaf. As result these values be 150 mM potassium phosphate buffer, 7.00, 0.18 mM, respectively. partially purified with specific 1.640 EU mg-1 34.9% yield, 1.108-fold. This study first terms characterization