Results 271 to 280 of about 122,606 (315)
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Biochimica et Biophysica Acta (BBA) - General Subjects, 2013
With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Since GPxs have recently been reviewed under various aspects, we here ...
Brigelius Flohé R, MAIORINO, MATILDE
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With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Since GPxs have recently been reviewed under various aspects, we here ...
Brigelius Flohé R, MAIORINO, MATILDE
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Kinetics of glutathione peroxidase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1969Abstract The dependency of the reaction rate of purified glutathione peroxidase (GSH: H2O2 oxidoreductase, EC 1.11.1.9) on the concentration of the substrates is investigated employing methods by which the substrates involved are determined immediately. GSH is measured polarographically. H2O2 is estimated by enzymatic oxidation of the fluorescent dye
Leopold Flohé, Ingeborg Brand
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Gastrointestinal glutathione peroxidase
BioFactors, 1999AbstractThe gastrointestinal glutathione peroxidase (GI‐GPx) is the fourth member of the GPx family. In rodents, it is exclusively expressed in the gastrointestinal tract, in humans also in liver. It has, therefore, been discussed to function as a primary barrier against the absorption of ingested hydroperoxides.
Kirstin Wingler, Regina Brigelius-Flohé
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[47] Phospholipid hydroperoxide glutathione peroxidase
Phosphorus and Sulfur and the Related Elements, 1988In acute inflammation the activated leukocytes generate cytotoxic oxygen free radicals. The role of these radical species in the cellular damage following an acute inflammatory reaction is well known. On the other hand the extent of the cellular damage must be dependent on both the rate of the free-radical generation and the scavenging capacity of the ...
MAIORINO, MATILDE +2 more
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The Catalytic Site of Glutathione Peroxidases
Antioxidants & Redox Signaling, 2008In GPxs, the redox-active Se or S, is at hydrogen bonding distance from Gln and Trp residues that contribute to catalysis. From sequence homology of >400 sequences and modeling of the DmGPx as a paradigm, Asn136 emerged as a fourth essential component of the active site.
TOSATTO, SILVIO +8 more
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Physiologia Plantarum, 1997
Oxidative stress in plants causes the induction of several enzymes, including superoxide dismutase (EC 1.15.1.1), ascorbate peroxidase (EC 1.11.1.11) and glutathione reductase (EC 1.6.4.2). The first two are responsible for converting superoxide to H2O2 and its subsequent reduction to H2O, and the third is involved in recycling of ascorbate ...
Gozal Ben-Hayyim +3 more
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Oxidative stress in plants causes the induction of several enzymes, including superoxide dismutase (EC 1.15.1.1), ascorbate peroxidase (EC 1.11.1.11) and glutathione reductase (EC 1.6.4.2). The first two are responsible for converting superoxide to H2O2 and its subsequent reduction to H2O, and the third is involved in recycling of ascorbate ...
Gozal Ben-Hayyim +3 more
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Cellular and Molecular Life Sciences, 2001
There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
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There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
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[5] Diversity of glutathione peroxidases
1995Publisher Summary This chapter focuses on the diversity of glutathione peroxidases. Selenium was identified as a toxic factor for grazing animals in the first half of the twentieth century and since then has been considered hazardous. Only long after the identification of the first selenoenzymes in bacteria and mammals was a Recommended Dietary ...
URSINI, FULVIO +6 more
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Selenoglutaredoxin as a Glutathione Peroxidase Mimic
ChemBioChem, 2008AbstractGlutaredoxin (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 (
Gerard Roelfes +2 more
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Reaction of cyanide with glutathione peroxidase
Biochemical and Biophysical Research Communications, 1980An oxidized form of ovine erythrocyte GSH peroxidase (Form C) that contains bound glutathione in equimolar ratio to the enzyme selenium is inactivated by cyanide. When Form C was treated with 1 or 10 mM KCN at pH 7.5, there was a rapid increase in ultraviolet absorption at 250 nm, S-cyanoglutathione was released, and the enzyme was reduced, as shown by
Howard E. Ganther, Richard J. Kraus
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