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Glutathione

ANZ Journal of Surgery, 2003
Glutathione (GSH) is an ubiquitous thiol‐containing tripeptide that plays a key role in cell biology. It modulates cell response to redox changes associated with the reactive oxygen species, detoxifies the metabolites of drugs; regulates gene expression and apop­tosis, and is involved in the transmembrane transport of organic solutes.
Heather, Jefferies   +5 more
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Glutathione and glutathione derivatives in immunotherapy

Biological Chemistry, 2016
Abstract Reduced glutathione (GSH) is the most prevalent non-protein thiol in animal cells. Its de novo and salvage synthesis serves to maintain a reduced cellular environment, which is important for several cellular functions. Altered intracellular GSH levels are observed in a wide range of pathologies, including several viral ...
FRATERNALE, ALESSANDRA   +2 more
openaire   +3 more sources

Glutathione

2015
Glutathione is an endogenous peptide with antioxidant and other metabolic functions. The nomenclature, formulae, elemental composition, and appearance and uses of the drug are included. The methods used for the synthesis and biosynthesis of glutathione are described.
Amer M, Alanazi   +2 more
openaire   +2 more sources

Reactions of glutathione and glutathione radicals with benzoquinones

Free Radical Biology and Medicine, 1992
The reactions of glutathione (GSH) and glutathione radicals with a series of methyl-substituted 1,4-benzoquinones and 1,4-benzoquinone have been studied. It was found that by mixing excess benzoquinone with glutathione at pH above 6.5, the products formed were complex and unstable. All of the other experiments were carried out at pH 6.0, where the main
J, Butler, B M, Hoey
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Transport of glutathione and glutathione conjugates by MRP1

Trends in Pharmacological Sciences, 2006
Glutathione (GSH)-conjugated xenobiotics and GSH-conjugated metabolites (e.g. the cysteinyl leukotriene C4) must be exported from the cells in which they are formed before they can be eliminated from the body or act on their cellular targets. This efflux is often mediated by the multidrug resistance protein 1 (MRP1) transporter, which also confers drug
Susan P C, Cole, Roger G, Deeley
openaire   +2 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

Glutathione and glutathione analogues; Therapeutic potentials

Biochimica et Biophysica Acta (BBA) - General Subjects, 2013
Glutathione (GSH) and related enzymes are critical to cell protection from toxins, both endogenous and environmental, including a number of anti-cancer cytotoxic agents.Enhancing GSH and associated enzymes represents a longtime and persistent aim in the search for cytoprotective strategies against cancer, neurologic degeneration, pulmonary and ...
Jian Hui, Wu, Gerald, Batist
openaire   +2 more sources

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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Glutathione and glutathione metabolizing enzymes in yeasts

Antonie van Leeuwenhoek, 1988
Total glutathione content, glutathione peroxidase, glutathione transferase and glutathione reductase activities have been measured in 12 species of yeasts. All the strains tested contained glutathione, though in different amounts, as well as the above mentioned enzymes.
CASALONE, ENRICO   +3 more
openaire   +3 more sources

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   +5 more
openaire   +2 more sources

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