Results 281 to 290 of about 618,316 (340)
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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
O. Griffith
semanticscholar +4 more sources
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
O. Griffith
semanticscholar +4 more sources
Biochimica et Biophysica Acta (BBA) - General Subjects, 2013
With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Since GPxs have recently been reviewed under various aspects, we here ...
R. Brigelius-Flohé, M. Maiorino
semanticscholar +3 more sources
With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Since GPxs have recently been reviewed under various aspects, we here ...
R. Brigelius-Flohé, M. Maiorino
semanticscholar +3 more sources
Glutathione and glutathione derivatives in immunotherapy
Biological Chemistry, 2016Abstract 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
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Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Journal of Laboratory and Clinical Medicine, 1967An assay procedure is described in which blood cell glutathione peroxidase may be accurately measured by a direct spectrophotometric procedure. Glutathione peroxidase activity is found to be associated with a relatively stable, nondialyzable, heat-labile,
D. Paglia, W. N. Valentine
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ASCORBATE AND GLUTATHIONE: Keeping Active Oxygen Under Control.
Annual Review of Plant Physiology and Plant Molecular Biology, 1998To cope with environmental fluctuations and to prevent invasion by pathogens, plant metabolism must be flexible and dynamic. Active oxygen species, whose formation is accelerated under stress conditions, must be rapidly processed if oxidative damage is ...
G. Noctor, C. Foyer
semanticscholar +1 more source
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 (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
openaire +2 more sources
Critical reviews in biochemistry and molecular biology, 1995
The glutathione S-transferases (GST) represent a major group of detoxification enzymes. All eukaryotic species possess multiple cytosolic and membrane-bound GST isoenzymes, each of which displays distinct catalytic as well as noncatalytic binding ...
J. Hayes, D. Pulford
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The glutathione S-transferases (GST) represent a major group of detoxification enzymes. All eukaryotic species possess multiple cytosolic and membrane-bound GST isoenzymes, each of which displays distinct catalytic as well as noncatalytic binding ...
J. Hayes, D. Pulford
semanticscholar +1 more source
Degradation of glutathione and glutathione conjugates in plants
Journal of Experimental Botany, 2023Abstract Glutathione (GSH) is a ubiquitous, abundant, and indispensable thiol for plants that participates in various biological processes, such as scavenging reactive oxygen species, redox signaling, storage and transport of sulfur, detoxification of harmful substances, and metabolism of several compounds.
Takehiro Ito, Naoko Ohkama-Ohtsu
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Selenium: biochemical role as a component of glutathione peroxidase.
Science, 2009When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H(2)O(2), added glutathione failed to protect the hemoglobin from oxidative damage.
J. T. Rotruck +5 more
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Glutathione and glutathione metabolizing enzymes in yeasts
Antonie van Leeuwenhoek, 1988Total 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
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