Results 241 to 250 of about 48,461 (279)

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, K, Schulze-Osthoff, S, Mihm, D, Galter, H, Schenk, H P, Eck, S, Roth, H, Gmünder   +7 more
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Thiol−Disulfide Exchange between Glutaredoxin and Glutathione

Biochemistry, 2010
Glutaredoxins 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, Andersen, Peter Anders, Jensen, Kristine Steen, Winther, Jakob R., Sigurskjold, Bent Walther   +4 more
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Measurement of Glutathione and Glutathione Disulfide

Current Protocols in Toxicology, 1999
AbstractMeasurements 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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Mechanisms of glutathione disulfide efflux from erythrocytes

Biochemical Pharmacology, 2012
Glutathione (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.
Irina, Ellison, John P, Richie
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Hypoxia increases plasma glutathione disulfide in rats

Lung, 1989
We tested the hypothesis that hypoxia causes cellular oxidative stress by measuring plasma concentrations of glutathione disulfide (GSSG) in rats exposed to acute and subacute hypoxia. In awake, unanesthetized, catheter-implanted rats, exposure to 8% O2 for 10 min caused pulmonary vasoconstriction and increased plasma GSSG. This increase in plasma GSSG
S W, Chang, T J, Stelzner, J V, Weil, N F, Voelkel   +3 more
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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
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Glutathione Disulfide Variability in Normal Human Blood

Analytical Biochemistry, 1994
A prevailing opinion is that glutathione disulfide (GSSG) levels in human blood are very low, but many studies have reported variable results. Therefore, our objective was to determine valid processing conditions for GSSG measurement and apply them to normal human blood samples.
B J, Mills, J P, Richie, C A, Lang
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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, C, Muckel, T P, Akerboom, H, Sies   +3 more
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Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine

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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Effect of the glutathione/glutathione disulfide redox couple on thiopurine methyltransferase

Biochemical Pharmacology, 2001
The 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
R A, Lysaa , D J, Warren, I, Sylte, J, Aarbakke   +3 more
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