Purification and properties of glutathione peroxidase from human placenta.

@article{Awasthi1979PurificationAP,
  title={Purification and properties of glutathione peroxidase from human placenta.},
  author={Y. Awasthi and D. D. Dao and A. Lal and S. Srivastava},
  journal={The Biochemical journal},
  year={1979},
  volume={177 2},
  pages={
          471-6
        }
}
Glutathione peroxidase (glutathione--H2O2 oxidoreductase; EC 1.11.1.9) was purified to homogeneity from human placenta by using (NH4)2SO4 precipitation, ion-exchange chromatography, Sephadex gel filtration and preparative polyacrylamide-disc-gel electrophoresis. Glutathione peroxidase from human placenta is a tetramer, having 4g-atoms of selenium/mol of protein. The molecular weight of the enzyme is about 85000 with a subunit size of about 22,000. Kinetic properties of the enzyme are described… Expand
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