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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
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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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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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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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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The development of glutathione S-transferase and glutathione peroxidase activities in human lung
Biochimica Et Biophysica Acta - General Subjects, 1986 The development of glutathione S-transferase and glutathione peroxidase activities has been studied in human lung cytosols. Whilst no clear change in glutathione peroxidase activity was identified, expression of the acidic glutathione S-transferase ...
Anthony A Fryer, R Hume, R C Strange
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The glutathione S-transferases of fish
Fish Physiology and Biochemistry, 1987Substantial soluble glutathione S-transferase activity and millimolar reduced glutathione (GSH) are present in most tissues of both teleosts and elasmobranchs. The hepatic enzymes of fish conjugate a range of electrophilic substrates with GSH, although their specificities are less broad than those of the transferases in rodent liver.
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Lung, 1984
Glutathione S-transferases play a major role in the protection of tissues from the toxic effects of exnobiotics and the products of lipid peroxidation. In the present studies we demonstrate that human lung has two forms of glutathione (GSH) S-transferase having isoelectric pH of 4.9 and 9.2.
C A, Partridge, D D, Dao, Y C, Awasthi
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Glutathione S-transferases play a major role in the protection of tissues from the toxic effects of exnobiotics and the products of lipid peroxidation. In the present studies we demonstrate that human lung has two forms of glutathione (GSH) S-transferase having isoelectric pH of 4.9 and 9.2.
C A, Partridge, D D, Dao, Y C, Awasthi
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