Results 311 to 320 of about 487,455 (339)
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Glutathione peroxidase and oxidative stress
Toxicology Letters, 1995In this study, overexpression of the cDNA for the major cytoplasmic glutathione peroxidase isoenzyme, GSH Peroxidase 1 (GSHPx-1), in human MCF-7 breast cancer cells has been shown to significantly increase the tolerance of these cells to oxidative stress produced by hydrogen peroxide or by the redox cycling of the quinone-containing anticancer agent ...
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Inactivation of Glutathione Peroxidase by Peroxynitrite
Archives of Biochemistry and Biophysics, 1998Glutathione peroxidase (GSH-Px) is inactivated on exposure to peroxynitrite under physiologically relevant conditions. Stopped-flow kinetic studies show that the reaction between peroxynitrite and GSH-Px is first-order in each of the reactants, with an apparent second-order rate constant of 4.5 +/- 0.2 x 10(4) M-1 s-1 per monomer unit of enzyme.
Giuseppe L. Squadrito +2 more
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[53] Glutathione peroxidase and hydroperoxides
1978Publisher Summary Gluthatione peroxidase is assayed by a modification of the method of Paglia and Valentine. Glutathione peroxidase catalyzes the reduction of hydroperoxides with glutathione as the reductant. The simple method is a spectrophotometric assay in which the reduction of GSSG is coupled to the oxidation of NADPH through glutathione ...
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Erythrocyte Glutathione‐Peroxidase Deficiency
British Journal of Haematology, 1970Summary Glutathione peroxidase deficiency is the most recently described erythrocyte enzyme abnormality. This enzyme occupies a critical position in the pathways leading to the decomposition of peroxides in the erythrocyte. On the basis of our studies of patients with GSH‐P deficiency, it appears that a spectrum of disease quite similar to that found ...
Dorothy Cameron +2 more
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The glutathione peroxidase family: Discoveries and mechanism.
Free Radical Biology & Medicine, 2022L. Flohé, S. Toppo, L. Orian
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Regulation of Glutathione Peroxidases
1997The glutathione peroxidases (GPx) belong to a superfamily of phylogenetically related proteins of diverse functions.1 The members of the superfamily containing a selenocysteine residue in their catalytic centers are highly efficient peroxidases reacting with a variety of hydroperoxides at rate constants of greater than 106 M-1 s-1.1 A cysteine residue ...
Leopold Flohé +2 more
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Electrophoretic polymorphism of glutathione peroxidase
Annals of Human Genetics, 1974SUMMARYA method for the detection of glutathione peroxidase after electrophoresis on starch gel has been devised. Blood samples from 780 persons of Caucasian or Negro origin were studied. An electrophoretically fast enzyme, designated as the Thomas variant, was found in 6·4 % of 392 Negro donors and 0·8 % of 388 Caucasian donors.
Carol West +2 more
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Homocysteine and Glutathione Peroxidase-1
Antioxidants & Redox Signaling, 2007Mildly elevated homocysteine levels (Hcy) increase the risk for atherothrombotic vascular disease in the coronary, cerebrovascular, and peripheral arterial circulations. The molecular mechanisms responsible for decreased bioavailability of endothelium-derived nitric oxide (NO) by Hcy involve an increase of vascular oxidant stress and inhibition of ...
Diane E. Handy +2 more
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A pseudogene for human glutathione peroxidase
Gene, 1992Glutathione peroxidases (GPx) serve a bioprotective function in the reduction of peroxides to less toxic substances. Both cellular and secreted forms of the protein have been reported, as well a number of distinct cDNA sequences. Previous efforts have described three distinct loci on human chromosomes 3, 21 and X which hybridize to a GPX cDNA and these
Alan M. Diamond +3 more
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Phylogenetic distribution of glutathione peroxidase
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19791. The enzyme glutathione peroxidase (E.C.1.11.1.9), known to be a selenoprotein from mammalian sources, was detected in the following vertebrates: fish, frog, salamander, and turtle. 2. Among invertebrates, the enzyme was detected in crayfish and snail but not in insects or earthworm. 3.
A. Shrift, J. Smith
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