Results 191 to 200 of about 429,903 (236)
Accumulation of the phytoalexin glyceollin i in soybean nodules infected by a bradyrhizobium-japonicum-nifa mutant [PDF]
Fischer, H.+3 more
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Analytical Biochemistry, 1980
Abstract The total glutathione content of biological samples is conveniently determined with an enzymatic recycling assay based on glutathione reductase ( F. Tietze, 1969 , Anal. Biochem. 27 , 502–522). In the original and several subsequent descriptions of this procedure, glutathione disulfide is selectively determined by assaying samples in which
O. Griffith
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Abstract The total glutathione content of biological samples is conveniently determined with an enzymatic recycling assay based on glutathione reductase ( F. Tietze, 1969 , Anal. Biochem. 27 , 502–522). In the original and several subsequent descriptions of this procedure, glutathione disulfide is selectively determined by assaying samples in which
O. Griffith
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1985
Publisher Summary Glutathione reductase is a flavoprotein catalyzing the NADPH-dependent reduction of glutathione disulfide (GSSG) to glutathione (GSH). The reaction is essential for the maintenance of glutathione levels. Glutathione has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other ...
Bengt Mannervik, Inger Carlberg
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Publisher Summary Glutathione reductase is a flavoprotein catalyzing the NADPH-dependent reduction of glutathione disulfide (GSSG) to glutathione (GSH). The reaction is essential for the maintenance of glutathione levels. Glutathione has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other ...
Bengt Mannervik, Inger Carlberg
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Glutathione Reductase and Ascorbate Peroxidase
Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants, 2019Gary Creissen+3 more
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The structure of the flavoenzyme glutathione reductase [PDF]
The three-dimensional structure of the dimeric flavoenzyme glutathione reductase from human erythrocytes has been elucidated by an X-ray diffraction analysis at 0.3 nm resolution. The polypeptide chain has been traced, and the binding positions of FAD, NADP and glutathione have been determined. A mechanism for the electron transfer is discussed.
Schulz, G.+3 more
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Glutathione reductase in evolution
Journal of Molecular Evolution, 1983The disulfide reducing activities of GSSG-and CoASSG-reductases were measured on partially purified extracts from a variety of prokaryotes and eukaryotes. Glutathione-reductase was found in varying amounts in all eukaryotes and prokaryotes, used in this study, with the exception of the two strict anaerobes Clostridium tartarivorum and Desulfovibrio ...
M. Ondarza, R. N. Ondarza, J. L. Rendón
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Inhibition of glutathione disulfide reductase by glutathione
Archives of Biochemistry and Biophysics, 1991Rat-liver glutathione disulfide reductase is significantly inhibited by physiological concentrations of the product, glutathione. GSH is a noncompetitive inhibitor against GSSG and an uncompetitive inhibitor against NADPH at saturating concentrations of the fixed substrate.
Hiram F. Gilbert+2 more
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Proteins: Structure, Function, and Bioinformatics, 2008
AbstractThioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 Å resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues.
ANGELUCCI, Francesco+5 more
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AbstractThioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 Å resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues.
ANGELUCCI, Francesco+5 more
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Reduction of a Trisulfide Derivative of Glutathione by Glutathione Reductase
Biochemical and Biophysical Research Communications, 1994Glutathione trisulfide was synthesized from glutathione disulfide and its reduction by glutathione reductase was studied. A two-step reaction was observed. In a first step, the rate of reduction was similar to that observed with glutathione disulfide.
Moutiez, M.+5 more
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Physiologia Plantarum : An International Journal for Plant Biology, 2018
The role of glutathione reductase (GR; EC 1.6.4.2) in the tolerance of Chlamydomonas reinhardtii P.A. Dangeard to high-intensity light stress (HL, 1400 μmol m-2 s-1 ) was examined.
Tsen-Hung Lin+8 more
semanticscholar +1 more source
The role of glutathione reductase (GR; EC 1.6.4.2) in the tolerance of Chlamydomonas reinhardtii P.A. Dangeard to high-intensity light stress (HL, 1400 μmol m-2 s-1 ) was examined.
Tsen-Hung Lin+8 more
semanticscholar +1 more source