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Science 9 February 1973:
Vol. 179. no. 4073, pp. 588 - 590
DOI: 10.1126/science.179.4073.588
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Articles

Selenium: Biochemical Role as a Component of Glutathione Peroxidase

J. T. Rotruck 1, A. L. Pope 2, H. E. Ganther 3, A. B. Swanson 4, D. G. Hafeman 4, and W. G. Hoekstra 5

1 Departments of Biochemistry and Meat and Animal Science, College of Agricultural and Life Sciences, University of Wisconsin, Madison 53706
2 Department of Meat and Animal Science
3 Department of Nutritional Sciences
4 Department of Biochemistry
5 Departments of Biochemistry and Nutritional Sciences

When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H2O2, added glutathione failed to protect the hemoglobin from oxidative damage. This occurred because the erythrocytes were practically devoid of glutathione-peroxidase activity. Extensively purified preparations of glutathione peroxidase contained a large part of the 75Se of erythrocytes labeled in vivo. Many of the nutritional effects of selenium can be explained by its role in glutathione peroxidase.


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