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Glutathione-S-transferase family of enzymes.
Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 2001The loci encoding the glutathione-S-transferase (GST) enzymes comprise a large supergene family located on at least seven chromosomes. The function of the GST enzymes has traditionally been considered to be the detoxication of electrophiles by glutathione conjugation. A wide variety of endogenous (e.g.
Richard C. Strange +3 more
semanticscholar +3 more sources
1996
Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
A, Raha, K D, Tew
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Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
A, Raha, K D, Tew
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Human Glutathione S-Transferases
Seminars in Liver Disease, 1998Human glutathione S-transferases (GSTs) are a functionally diverse family of soluble enzymes of detoxification that use reduced glutathione (GSH) in conjugation and reduction reactions. Toxic electrophiles, including a variety of carcinogens, are substrates for the GSTs and after conjugation or reduction they are more easily excreted into bile or urine.
R, Whalen, T D, Boyer
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Human glutathione S-transferases
International Journal of Biochemistry, 19941. Multiple forms of glutathione S-transferase (GST) isoenzymes present in human tissues are dimers of subunits belonging to three distinct gene families namely alpha, mu and pi. Only the subunits within each class hybridize to give active dimers. 2.
Y C, Awasthi, R, Sharma, S S, Singhal
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Marine Glutathione S-Transferases
Marine Biotechnology, 2007The aquatic environment is generally affected by the presence of environmental xenobiotic compounds. One of the major xenobiotic detoxifying enzymes is glutathione S-transferase (GST), which belongs to a family of multifunctional enzymes involved in catalyzing nucleophilic attack of the sulfur atom of glutathione (gamma-glutamyl-cysteinylglycine) to an
Brian, Blanchette +2 more
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Drosophila Glutathione S‐Transferases
2005The Drosophila glutathione S-transferases (GSTs; EC2.5.1.18) comprise a host of cytosolic proteins that are encoded by a gene superfamily and a homolog of the human microsomal GST. Biochemical studies of certain recombinant GSTs have linked their enzymatic functions to important substrates such as the pesticide DDT and 4-hydroxynonenal, a reactive ...
Chen-Pei D, Tu, Bünyamin, Akgül
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Low glutathione S -transferase dogs
Archives of Toxicology, 2004Liver and kidney glutathione S-transferase (GST) activities to 1,2-dichloro-4-nitrobenzene (DCNB) as a substrate (GST-D activities) were measured in 280 dogs from five different breeders, and significant individual differences in this activity were observed in both organs. Interestingly, 34 out of the 280 dogs (i.e. 12.1%) were those in which liver GST-
Toshiyuki, Watanabe +4 more
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Glutathione S-Transferases - A Review
Current Medicinal Chemistry, 1999Abstract: The Glutathione S-transferases (GSTs) form a group of multi-gene isoenzymes involved in the cellular detoxification of both xenobiotic and endobiotic compounds. GSTs have been divided into a number of subclasses, alpha (α), mu {μ), pi (π), and theta (θ).
A E, Salinas, M G, Wong
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Particle-Bound Glutathione-S-Transferases
Enzyme, 1979The incubation of liver microsomes or mitochondria with glutathione, in the presence of electrophilic compounds, decreased the glutathione concentration in the incubation medium. Product analysis revealed that glutathione conjugates were formed.
P, Kraus, B, Gross
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1977
Any symposium which deals with the metabolic formation and inactivation of reactive metabolites must necessarily consider the prominent role played by glutathione (GSH) and the glutathione transferases since this simple tripeptide (Fig. 1) and the enzymes which employ GSH as a cosubstrate represent a very important factor in the protection of cellular ...
Donald M. Jerina, John R. Bend
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Any symposium which deals with the metabolic formation and inactivation of reactive metabolites must necessarily consider the prominent role played by glutathione (GSH) and the glutathione transferases since this simple tripeptide (Fig. 1) and the enzymes which employ GSH as a cosubstrate represent a very important factor in the protection of cellular ...
Donald M. Jerina, John R. Bend
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