Purification and properties of human erythrocyte glutathione peroxidase.

@article{Awasthi1975PurificationAP,
  title={Purification and properties of human erythrocyte glutathione peroxidase.},
  author={Y. Awasthi and E. Beutler and S. Srivastava},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 13},
  pages={
          5144-9
        }
}
Glutathione peroxidase has been purified to homogeneity from human erythrocytes. The purification steps involved ammonium sulfate precipitation of hemolysate, CM-cellulose (CM-52), DEAE-cellulose (DE52), Sephadex G-200, and DEAE-Sephadex column chromatography. In the last step, i.e. DEAE-Sephadex A-25 column chromatography, the enzyme was eluted in a major peak and tailing fraction. The major peak was found to be homogeneous on polyacrylamide disc electrophoresis and disignated as glutathione… Expand
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