Results 211 to 220 of about 89,068 (261)

Reduction of a Trisulfide Derivative of Glutathione by Glutathione Reductase

Biochemical and Biophysical Research Communications, 1994
Glutathione 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., Aumercier, M., Teissier, E., Parmentier, B., Tartar, A., Sergheraert, C.   +5 more
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Glutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase

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, MIELE, Adriana Erica, BOUMIS, Giovanna, DIMASTROGIOVANNI, Daniela, BRUNORI, Maurizio, BELLELLI, Andrea   +5 more
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The structure of the flavoenzyme glutathione reductase

Nature, 1978
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., Schirmer, R., Sachsenheimer, W., Pai, E.   +3 more
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Inhibition of glutathione reductase by oncomodulin

Archives of Biochemistry and Biophysics, 1990
Evidence for a specific interaction between oncomodulin and glutathione reductase is presented. Glutathione reductase (EC 1.6.4.2) isolated from either the bovine intestinal mucosa or the rat liver was bound in a Ca2(+)-dependent manner to oncomodulin which was covalently attached to Sepharose.
Palmer, E., Macmanus, J., Mutus, B.
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Ageing of Glutathione Reductase in the Lens

Experimental Eye Research, 1994
The distribution of glutathione reductase activity in concentric layers from the lens has been determined as a function of age for 16 species. Primate lenses have almost ten times the level of glutathione reductase found in other species. Comparison with the activity of hexokinase revealed that this is not due to a higher overall rate of metabolism in ...
W Z, Zhang, R C, Augusteyn
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Interaction of nitrofurans with glutathione reductase

Biochimica et Biophysica Acta (BBA) - General Subjects, 1991
Nitrofurans inhibit the oxidation of NADPH by glutathione, catalyzed by yeast glutathione reductase (EC 1.6.4.2). acting as uncompetitive incomplete inhibitors for NADPH and glutathione. The quinoline-substituted nitrofurans were the most effective inhibitors.
N K, Cénas, D A, Bironaité, J J, Kulys, N M, Sikhova   +3 more
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Glutathione reductase functions as vanadate(V) reductase

Archives of Biochemistry and Biophysics, 1990
The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvement of the superoxide radical. The vanadate(V) reduction was found to
X L, Shi, N S, Dalal
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Measurement of Glutathione Reductase Activity

Current Protocols in Toxicology, 1999
AbstractReduced glutathione, a thiol, is essential to the survival of the cells of most aerobic organisms. It is present intracellularly and provides protection from hydroperoxides and free radicals. This unit describes a continuous spectrophotometric assay for reductase activity: it follows the reduction of glutathione disulfide to reduced glutathione
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Glutathione Peroxidase and Glutathione Reductase Activities toward Glutathione-Derived Antioxidants

Biochemical and Biophysical Research Communications, 1994
A new class of glutathione derivatives with antioxidant properties has been prepared by transformation of the NH2 group into a pyrrole ring with various substitutions at the 2 and 5 positions. Due to steric hindrance and/or hydrophobicity of the 2-5-disubstituted pyrrole ring, the reduced glutathione derivatives are poor substrates of the glutathione ...
J M, Gaullier, P, Lafontant, A, Valla, M, Bazin, M, Giraud, R, Santus   +5 more
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Gene duplication in glutathione reductase

Journal of Molecular Biology, 1980
Abstract The two nucleotide-binding domains of the flavo-enzyme glutathione reductase have similar chain folds. In order to evaluate whether the observed similarity is significant or not, a mean distance between both chains after best overlay was calculated. Insertions and deletions were taken into account. The significance of the observed similarity
openaire   +3 more sources