Results 321 to 330 of about 77,313 (353)
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Measurement of Glutathione and Glutathione Disulfide
Current Protocols in Toxicology, 1999AbstractMeasurements of glutathione should include quantification of both the reduced and oxidized forms. HPLC‐based assays for glutathione and other cellular thiols and disulfides utilize a variety of detection methods, including ultraviolet, fluorescence, and electrochemical methods.
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Glutathionylation of proteins by glutathione disulfide S-oxide
Biochemical Pharmacology, 2002Aqueous solution of S-nitrosoglutathione (GSNO) underwent spontaneous chemical transformation that generated several glutathione derivatives including glutathione sulfonic acid (GSO3H), glutathione disulfide S-oxide (GS(O)SG), glutathione disulfide S-dioxide, and glutathione disulfide.
Freesia L. Huang, Kuo-Ping Huang
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Interactions of glutathione disulfide with lens crystallins
Current Eye Research, 1982The study was designed to investigate the formation of mixed disulfides (PSSG) of protein and glutathione (GSH) in the lens. The possibility that oxidized GSH reacts with lens protein sulfhydryls was examined by incubating tritiated glutathione disulfide ([3H] GSSG) with a solution of dialyzed water-soluble bovine lens crystallins.
M. K. Mostafapour, Venkat N. Reddy
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Determination of glutathione and glutathione disulfide in biological samples: An in-depth review
Journal of Chromatography B, 2009Glutathione (GSH) is a thiol-containing tripeptide, which plays central roles in the defence against oxidative damage and in signaling pathways. Upon oxidation, GSH is transformed to glutathione disulfide (GSSG). The concentrations of GSH and GSSG and their molar ratio are indicators of cell functionality and oxidative stress.
Monostori Péter +3 more
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Effect of the glutathione/glutathione disulfide redox couple on thiopurine methyltransferase
Biochemical Pharmacology, 2001The susceptibility of recombinant human thiopurine methyltransferase (hTPMT) to thiol-disulfide exchange was investigated. The enzyme was incubated in buffers of the redox couple GSH and GSSG. The values of the chosen concentrations and concentration ratios of the redox couple equaled those expected to occur in vivo. Activity measurements of the enzyme
Roy A. Lysaaa +3 more
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Talanta, 2021
In the present study we report the simultaneous determination of glutathione (GSH) and glutathione disulfide (GSSG) by an automated flow method based on the concept of zone fluidics. GSH is quantified selectively in a first run by reaction with o-phthalaldehyde at a mildly basic pH = 8, without interference from GSSG. The latter was also found to react
Apostolia Tsiasioti +1 more
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In the present study we report the simultaneous determination of glutathione (GSH) and glutathione disulfide (GSSG) by an automated flow method based on the concept of zone fluidics. GSH is quantified selectively in a first run by reaction with o-phthalaldehyde at a mildly basic pH = 8, without interference from GSSG. The latter was also found to react
Apostolia Tsiasioti +1 more
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Analytical Biochemistry, 1980
A rapid and sensitive high-performance liquid chromatography method for determination of nanomole levels of glutathione, glutathione disulfide, cysteine glutathione-mixed disulfide and 20 related sulfur-containing amino acids or their derivatives has been described.
D.W. Potter +5 more
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A rapid and sensitive high-performance liquid chromatography method for determination of nanomole levels of glutathione, glutathione disulfide, cysteine glutathione-mixed disulfide and 20 related sulfur-containing amino acids or their derivatives has been described.
D.W. Potter +5 more
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Visualization of the compartmentalization of glutathione and protein‐glutathione mixed disulfides in cultured cells [PDF]
The FASEB Journal, 2002 Fluorescence microscopy of A549 cells stained with a glutathione (L-gamma-glutamyl-L-cysteinylglycine, GSH)-specific polyclonal antibody displayed uniform staining of the peri-nuclear cytosol, with the nuclear region apparently lacking GSH staining.
Sten Orrenius +7 more
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Thiol−Disulfide Exchange between Glutaredoxin and Glutathione
Biochemistry, 2010Glutaredoxins are ubiquitous thiol-disulfide oxidoreductases which catalyze the reduction of glutathione-protein mixed disulfides. Belonging to the thioredoxin family, they contain a conserved active site CXXC motif. The N-proximal active site cysteine can form a mixed disulfide with glutathione or an intramolecular disulfide with the C-proximal ...
Iversen, Rasmus +4 more
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Mechanisms of glutathione disulfide efflux from erythrocytes
Biochemical Pharmacology, 2012Glutathione (GSH) plays numerous critical protective roles in the erythrocyte and GSH turnover is likely an important factor in regulating susceptibility to oxidative stress and toxins. Efflux of glutathione disulfide (GSSG) from erythrocytes is an important component in the regulation of GSH levels; however, little is known of the mechanisms involved.
John P. Richie, Irina Ellison
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