Journal ArticleDOI
Selenium: Biochemical Role as a Component of Glutathione Peroxidase
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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.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.read more
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Glutathione peroxidase activity in selenium-deficient rat liver☆
TL;DR: Two peaks of glutathione peroxidase activity were present in the Sephadex G-150 gel filtration chromatogram of rat liver supernatant when 1.5 mM cumene hydroperoxide was used as substrate, and the second peak represents a second glutathienase activity which catalyzes the destruction of organic hydroperoxides but has little activity toward H 2 O 2 and which persists in severe selenium deficiency.
Journal ArticleDOI
Glutathione and its role in cellular functions.
TL;DR: This article serves as introduction to the FRBM Forum on glutathione and emphasizes cellular functions: What is GSH?
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Organoselenium and Organotellurium Compounds: Toxicology and Pharmacology
TL;DR: The development of new organochalcogens with higher thiol-peroxidase activity that can use other non-toxic thiol reducing agents, such as N-acetylcysteine instead of glutathione, will permit the investigation of the co-administration of organochAlcogens and thiols as a formulation for antioxidant therapy.
Journal ArticleDOI
Nanozymes: Classification, Catalytic Mechanisms, Activity Regulation, and Applications
TL;DR: This review systematically introduces the classification, catalytic mechanism, activity regulation as well as recent research progress of nanozymes in the field of biosensing, environmental protection, and disease treatments, etc. in the past years.
References
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Journal Article
Improved method for the determination of blood glutathione.
Ernest Beutler,O Duron,B M Kelly +2 more
Journal ArticleDOI
Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown.
TL;DR: The most plausible route for the conversion of hemoglobin into biliverdin in vivo is through the oxidation and opening of the tetrapyrrole ring, after which the globin and iron are removed as discussed by the authors.
I. glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown*
TL;DR: Although the exact mechanism of the conversion of hemoglobin into biliverdin in vivo is still in doubt, the most plausible route is through the oxidation and opening of the tetrapyrrole ring, after which the globin and iron are removed.