Results 281 to 290 of about 122,606 (315)
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2011
Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE +5 more
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Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE +5 more
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[12] Assays of glutathione peroxidase
1984Publisher Summary To determine glutathione peroxidase reliably, some factors of potential pitfall have to be considered, for example, enzymatic side reactions of substrates (especially when crude tissue samples are assayed), high and variable spontaneous reaction rates of substrates, and the peculiar kinetics of the enzyme itself.
W. A. Günzler, Leopold Flohé
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The glutathione peroxidase activity of glutathione S-transferases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1980Glutatione 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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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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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, 2008Electrophoretically 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.
T. I. Rakhmanova +2 more
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Inhibition of glutathione peroxidase by coenzyme A
Biochemical and Biophysical Research Communications, 1970Abstract 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
Radu M. Olinescu +2 more
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Glutathione Peroxidase of Fish
Journal of Food Science, 1992ABSTRACTGlutathione peroxidase (GSH‐Px) activity was detected in the muscle and skin tissues from several fish species. The muscle GSH‐Px showed an optimum pH at 8.0 for salmon and 8.5 for carp. Stability of salmon muscle enzyme was enhanced in the presence of reduced glutathione (GSH), but considerably decreased in the presence of tert ...
Toshiki Nakano +2 more
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2018
Eight glutathione peroxidase (Gpx) genes have been identified in the human and mouse genomes. The conserved redox-active amino acid residue is selenocysteine in five of the human enzymes and cysteine in the others. Cysteine-containing murine Gpx6 is the only difference between mouse and man.
Marcus Conrad +1 more
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Eight glutathione peroxidase (Gpx) genes have been identified in the human and mouse genomes. The conserved redox-active amino acid residue is selenocysteine in five of the human enzymes and cysteine in the others. Cysteine-containing murine Gpx6 is the only difference between mouse and man.
Marcus Conrad +1 more
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2010
Seven glutathione peroxidase (Gpx) genes have been identified in the human and mouse genomes. The conserved redox-active amino acid residue is selenocysteine in most of the enzymes and cysteine in the others. The Gpxs vary in their reaction characteristics and distribution within the organism. Gpx1 is the most abundant and widely distributed Gpx. It is
K.E. Hill, R.F. Burk
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Seven glutathione peroxidase (Gpx) genes have been identified in the human and mouse genomes. The conserved redox-active amino acid residue is selenocysteine in most of the enzymes and cysteine in the others. The Gpxs vary in their reaction characteristics and distribution within the organism. Gpx1 is the most abundant and widely distributed Gpx. It is
K.E. Hill, R.F. Burk
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The Role of Glutathione Peroxidases in Trypanosomatids
Biological Chemistry, 2003Reactive 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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