Selenium: Biochemical Role as a Component of Glutathione Peroxidase
John T. Rotruck, A. L. Pope, Howard E. Ganther, Anne Swanson, Dean G. Hafeman, W. G. Hoekstra
Science
Abstract
When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H(2)O(2), 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 (75)Se of erythrocytes labeled in vivo. Many of the nutritional effects of selenium can be explained by its role in glutathione peroxidase.
Extracted Claims
2 claims extracted from this paper into the knowledge graph
glutathione peroxidase contains selenium
“Extensively purified preparations of glutathione peroxidase contained a large part of the (75)Se of erythrocytes labeled in vivo.”
glutathione peroxidase activity is required to protect hemoglobin from oxidative damage
“When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H(2)O(2), added glutathione failed to protect the hemoglobin from oxidative damage...”