Results 241 to 250 of about 53,702 (285)
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Determination of glutathione and glutathione disulfide using zone fluidics and fluorimetric detection

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
exaly   +3 more sources

Glutathionylation of proteins by glutathione disulfide S-oxide

Biochemical Pharmacology, 2002
Aqueous 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.
Kuo-Ping Huang, Freesia L Huang
exaly   +3 more sources

Glutathione amperometric detection based on a thiol–disulfide exchange reaction [PDF]

open access: yesAnalytica Chimica Acta, 2006
A method based on a thiol-disulfide exchange reaction is proposed for glutathione detection. The method utilises a reaction between glutathione and an excess of the disulfide cystamine which produces an equimolar concentration of the thiol cysteamine ...
Francesco Ricci   +2 more
exaly   +2 more sources

Determination of glutathione and glutathione disulfide in biological samples: An in-depth review [PDF]

open access: possibleJournal of Chromatography B, 2009
Glutathione (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
openaire   +3 more sources

Inhibition of glutathione disulfide reductase by glutathione

Archives of Biochemistry and Biophysics, 1991
Rat-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.
P M, Chung, R E, Cappel, H F, Gilbert
openaire   +2 more sources

Functions of glutathione and glutathione disulfide in immunology and immunopathology

The FASEB Journal, 1994
Even a moderate increase in the cellular cysteine supply elevates the intracellular glutathione (GSH) and glutathione disulfide (GSSG) levels and potentiates immunological functions of lymphocytes in vitro. At low GSSG levels, T cells cannot optimally activate the immunologically important transcription factor NF
W, Dröge   +7 more
openaire   +2 more sources

Inhibition of protein synthesis by glutathione disulfide in the presence of glutathione

Biochemical and Biophysical Research Communications, 1971
Abstract As little as 5 × 10−5 M glutathione disulfide (GSSG) in the presence of 80 × 10−5 M glutathione (GSH) in a rabbit reticulocyte lysate caused a profound inhibition of initiation of protein synthesis. A potential physiological regulatory role for GSSG in protein synthesis is thus revealed.
N S, Kosower   +4 more
openaire   +2 more sources

Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide

Biochemical Pharmacology, 1983
The amount of glutathione present in hepatic protein mixed disulfides was determined to be 20-30 nmole/g liver. This was established using two specific enzymatic methods: (a) the coupled assay with DTNB and glutathione (GSSG) reductase and (b) a newly developed test using GSH transferase and 1-chloro-2,4-dinitrobenzene for the estimation of GSH ...
R, Brigelius   +3 more
openaire   +2 more sources

Measurement of glutathione-protein mixed disulfides

International Journal of Radiation Oncology*Biology*Physics, 1984
We have undertaken the development of a sensitive and highly specific assay for the presence of mixed disulfides between protein thiol groups and endogenous thiols. Previous investigations on the concentrations of glutathione (GSH), glutathione disulfide (GSSG) and protein glutathione mixed disulfides (ProSSG) have been of limited usefulness because of
J C, Livesey, D J, Reed
openaire   +2 more sources

Interactions of glutathione disulfide with lens crystallins

Current Eye Research, 1982
The 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, V N, Reddy
openaire   +2 more sources

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