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

doi:10.1126/science.179.4073.588

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.

Keywords

SeleniumGlutathione peroxidaseGlutathionePeroxidaseGPX6GPX3Glutathione reductaseChemistryBiochemistryGPX4In vivoHemoglobinIn vitroGPX1EnzymeBiologyBiotechnology

Affiliated Institutions

University of Wisconsin–Madison US

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Publication Info

Year: 1973
Type: article
Volume: 179
Issue: 4073
Pages: 588-590
Citations: 7668
Access: Closed

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APA Style

                            
                                
                                    John T. Rotruck, 
                                
                                    A. L. Pope, 
                                
                                    Howard E. Ganther
                                
                                et al.
                            
                            (1973). 
                            Selenium: Biochemical Role as a Component of Glutathione Peroxidase. 
                            Science
                            , 179
                            (4073)
                            , 588-590.
                            https://doi.org/10.1126/science.179.4073.588
                        

Identifiers

DOI: 10.1126/science.179.4073.588