Abstract
A procedure for obtaining the electrophoretically and ultracentrifugally homogenous preparation of “methemoglobin reductase” from erythrocytes of blue-white dolphin was developed. Method consists of DEAE-cellulose adsorption, fractionation with ammonium sulfate, Sephadex G-75 gel filtration and DEAE-Sephadex A-50 column chromatography. There were obtained three preparations of enzyme. All these preparations strongly reduced methemoglobin, metmyoglobin and cytochrome c in the presence of methyleneblue when NADPH or NADH was used as the cofactor. The activity of NADPH as the cofactor was higher than that of NADH. The enzyme contained neither flavin nor heme, and molecular weight was 23, 000_??_28, 000.
