Results 341 to 350 of about 147,440 (362)
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Gene duplication in glutathione reductase
Journal of Molecular Biology, 1980Abstract 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
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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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Measurement of Glutathione Reductase Activity
Current Protocols in Toxicology, 1999AbstractReduced 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, 1994A 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 ...
P. Lafontant +5 more
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Elemental selenium and glutathione reductase
Medical Hypotheses, 1985Selenium is an essential trace element important to several metabolic processes, although selenium in the chemical form of elemental selenium (Se degree) is commonly believed to be biologically inert. Recent data shows that colloidal suspensions of red amorphous elemental selenium are more easily reduced than previously thought, and that such ...
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Immunolocalization of glutathione reductase in the murine brain
The Journal of Comparative Neurology, 1996Free radical species arise from the univalent reduction of oxygen. The cytosolic agent H2O2, produced during enzymatic scavenging of the superoxide radical (O2-) is in turn removed predominantly via the oxidation of reduced glutathione (GSH) to the oxidized form (GSSG) by glutathione peroxidase.
Jakob Korf +4 more
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FAD-binding site of glutathione reductase
Journal of Molecular Biology, 1982Abstract The FAD-binding site in dimeric glutathione reductase has been elucidated by application of sequence and X-ray analyses in parallel. The geometry was derived from a multiple isomorphous replacement map of 2 A resolution. FAD binds in a rather elongated conformation with the flavin portion in the centre of one subunit and the adenine portion ...
Schulz, G., Schirmer, R., Pai, E.
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Regulation of horse-liver glutathione reductase
International Journal of Biochemistry, 19931. The enzyme was rapidly inactivated by NAD(P)H, GSH, dithionite or borohydride, while activity increased in the presence of NAD(P)+ or GSSG. NADH was more efficient for inactivation than NADPH. Redox inactivation required neutral or alkaline pH, was maximal at pH 8.5, and depended on the presence of metal cations. 2.
Juan López-Barea +4 more
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A role for glutathione and glutathione reductase in control of corneal hydration
Experimental Eye Research, 1984We have assessed the importance of the glutathione redox system of the corneal endothelial cells in the control of stromal hydration. The ability of freshly isolated corneas to maintain normal hydration during perfusion, while the activity of glutathione reductase was inhibited with 1.3-bis(2-chloroethyl)-1-nitrosourea (BCNU), was tested under a number
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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
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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
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