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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.
K, Wingler, R, Brigelius-Flohé
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2013
Class III peroxidases are heme-containing proteins of the secretory pathway with an extremely high number of isoenzymes, indicating the tremendous and important functions of this protein family. This chapter describes fractionation of the cell in subproteomes, their separation by polyacrylamide gel electrophoresis (PAGE) and visualization of peroxidase
Sabine, Lüthje +5 more
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Class III peroxidases are heme-containing proteins of the secretory pathway with an extremely high number of isoenzymes, indicating the tremendous and important functions of this protein family. This chapter describes fractionation of the cell in subproteomes, their separation by polyacrylamide gel electrophoresis (PAGE) and visualization of peroxidase
Sabine, Lüthje +5 more
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Molecular and Cellular Biochemistry, 1981
Horseradish peroxidase C (HRP; ferric) reacts with H2O2 to form Compound I, with an equilibrium constant of about 10(14) M-1. Two-step reduction of Compound I to Compound II and further to the ferric enzyme occurs reversibly at Eo' values of 0.90 and 0.93 V (pH 7.0), respectively.
I, Yamazaki, M, Tamura, R, Nakajima
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Horseradish peroxidase C (HRP; ferric) reacts with H2O2 to form Compound I, with an equilibrium constant of about 10(14) M-1. Two-step reduction of Compound I to Compound II and further to the ferric enzyme occurs reversibly at Eo' values of 0.90 and 0.93 V (pH 7.0), respectively.
I, Yamazaki, M, Tamura, R, Nakajima
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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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Common phylogeny of catalase-peroxidases and ascorbate peroxidases
Gene, 2000Catalase-peroxidases belong to Class I of the plant, fungal, bacterial peroxidase superfamily, together with yeast cytochrome c peroxidase and ascorbate peroxidases. Obviously these bifunctional enzymes arose via gene duplication of an ancestral hydroperoxidase. A 230-residues long homologous region exists in all eukaryotic members of Class I, which is
M, Zámocký, S, Janecek, F, Koller
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Applied Microbiology and Biotechnology, 2014
The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P.
Nancy, Coconi-Linares +5 more
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The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P.
Nancy, Coconi-Linares +5 more
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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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Lignin peroxidase-type activity of soybean peroxidase
Enzyme and Microbial Technology, 1995Soybean peroxidase (SBP), an acidic peroxidase isolated from the hulls of the bean, catalyzes the efficient oxidation of veratryl alcohol to veratraldehyde in the presence of H2O2. The reaction is optimal at pH 2.4 in the presence of 0.2 m CaCl2. Soybean peroxidase is highly thermostable at pH 2.4, with half-lives of 210 and 2.5 h at 30 and 50°C ...
James P. McEldoon +2 more
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Class I Heme Peroxidases: Characterization of Soybean Ascorbate Peroxidase
Archives of Biochemistry and Biophysics, 1998An efficient expression system [D. A. Dalton et al. Arch. Biochem. Biophys. 328, 1-8, 1996) for soybean nodule ascorbate peroxidase (APX) has, for the first time, been used to generate enzyme in large enough quantities for detailed biophysical analysis. The recombinant APX has been characterized by electronic absorption, EPR, NMR and circular dichroism
Jones, DK +3 more
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Archives of Biochemistry and Biophysics, 1952
Abstract The evidence for horse-radish peroxidase heme linkages has been reinvestigated in the acid region and there no longer exists experimental support for a heme-linked hydroxyl group. The formation of inactive compound B and the splitting of the enzyme terminate the activity of the enzyme.
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Abstract The evidence for horse-radish peroxidase heme linkages has been reinvestigated in the acid region and there no longer exists experimental support for a heme-linked hydroxyl group. The formation of inactive compound B and the splitting of the enzyme terminate the activity of the enzyme.
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