Results 251 to 260 of about 371,704 (300)

Inhibition of glutathione peroxidase by coenzyme A

Biochemical and Biophysical Research Communications, 1970
Abstract Glutathione peroxidase has been found to be extremely sensitive to inhibition by coenzyme A. Blocking the SH group of coenzyme A reduces the inhibitory effectiveness about 6-fold. It is thus possible that GSH peroxidase activity is regulated in vivo by the CoA/acyl CoA ratio. Dephospho-CoA was about 11-fold less effective than CoA, and
C, Little, R M, Olinescu, P J, O'Brien
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GLUTATHIONE PEROXIDASE LEVELS IN BRAIN

Journal of Neurochemistry, 1974
AbstractGlutathione peroxidase activity in brains of various animals was examined. Enzyme activity was low, approximately 10 nmol of glutathione oxidized min−1 mg protein−1 or less. This result suggests that brain tissues contain insufficient glutathione peroxidase activity to provide protection from peroxidative damage and that an alternative ...
O, De Marchena, M, Guarnieri, G, McKhann
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Selenoglutaredoxin as a Glutathione Peroxidase Mimic

ChemBioChem, 2008
AbstractGlutaredoxin (Grx1) from Escherichia coli is a monomeric, 85‐amino‐acid‐long, disulfide‐containing redox protein. A Grx1 variant in which the redox‐active disulfide was replaced with a selenocysteine (C11U/C14S) was prepared by native chemical ligation from three fragments as a potential mimic of the natural selenoenzyme glutathione peroxidase (
Casi G, Roelfes G, Hilvert D
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Erythrocyte Glutathione‐Peroxidase Deficiency

British Journal of Haematology, 1970
Summary 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 ...
T F, Necheles, M H, Steinberg, D, Cameron   +2 more
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Homocysteine and Glutathione Peroxidase-1

Antioxidants & Redox Signaling, 2007
Mildly 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 ...
Edith, Lubos, Joseph, Loscalzo, Diane E, Handy   +2 more
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The glutathione peroxidase activity of glutathione S-transferases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
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Glutathione Peroxidase 4 and Ferroptosis

2016
Glutathione peroxidase 4 (Gpx4) is one of eight members of the mammalian glutathione peroxidase family of enzymes. Gpx4 is unique due to its capacity to efficiently reduce phospholipid hydroperoxides. Additionally, it has been recognized that Gpx4 governs a novel form of non-apoptotic cell death, named ferroptosis.
Friedmann Angeli, J.P.F., Proneth, B., Conrad, M.   +2 more
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The Role of Glutathione Peroxidases in Trypanosomatids

Biological Chemistry, 2003
Reactive oxygen species are the unwanted by-products of aerobic metabolism. To protect cells against their potentially lethal effects a series of pathways have evolved that are collectively called the oxidative defence system. In most eukaryotes, catalases and selenium-dependent glutathione peroxidases form the front line of defence against ...
Shane R, Wilkinson, John M, Kelly
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Glutathione peroxidase and oxidative stress

Toxicology Letters, 1995
In 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 Benzaldehyde

Toxicology and Applied Pharmacology, 1996
Chronic benzaldehyde exposure is known to cause central nervous system (CNS) disturbances. Previous studies have shown that benzaldehyde causes the formation of reactive oxygen species (ROS) in rat synaptosomal fractions. Benzaldehyde has also been implicated in ROS formation in the CNS of rats treated with toluene.
T, Tabatabaie, R A, Floyd
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