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Glutathione peroxidases

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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Gastrointestinal glutathione peroxidase

BioFactors, 1999
AbstractThe 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.
K, Wingler, R, Brigelius-Flohé
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Kinetics of glutathione peroxidase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1969
Abstract 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
L, Flohé, I, Brand
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PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE

Phosphorus and Sulfur and the Related Elements, 1988
In 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, 2008
In 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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The glutathione peroxidases

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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Glutathione Peroxidase 4

2016
Glutathione peroxidase 4 (GPx4) is a selenocysteine (Sec)-containing glutathione peroxidase. GPx4 catalyzes the reduction of hydroperoxides and the oxidation of thiols through a ping-pong mechanism in which the redox transitions are faster than the formation of enzyme-substrate complexes; thus, K m and V max are infi nite.
MAIORINO, MATILDE   +8 more
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Isolation and purification of glutathione peroxidase

Applied Biochemistry and Microbiology, 2008
Electrophoretically homogeneous glutathione peroxidase (EC 1.11.1.9) preparation from rat liver with a specific activity of 1.46 U/mg of protein and a yield of 7.2% was obtained using the purification procedure developed. The K(M) values for reduced glutathione and hydrogen peroxide were 0.033 and 0.208 mM, respectively.
K K, Shul'gim   +2 more
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