Results 131 to 140 of about 21,538,465 (192)

Bioactivation of the β-Amyloid Precursor Protein-Cleaving Enzyme 1 Inhibitor Atabecestat Leads to Protein Adduct Formation on Glutathione S-Transferase Pi. [PDF]

Chem Res Toxicol
Ford M, Thomson PJ, Lister A, Snoeys J, Leclercq L, Cuyckens F, Naisbitt DJ, Meng X.   +7 more
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Study of Glutathione S-Transferase, Its Isoenzyme (Pi), and Tumor Markers (CA15-3, HE4) in Breast Carcinoma Patients (Before and After Treatment).

J Pharm Bioallied Sci
Hawale D, Abichandani L, Ambad R.
europepmc   +1 more source

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Glutathione S-Transferases

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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Human glutathione S-transferases

International Journal of Biochemistry, 1994
1. 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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Human Glutathione S-Transferases

Seminars in Liver Disease, 1998
Human 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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Glutathione S-Transferases - A Review

Current Medicinal Chemistry, 1999
Abstract: 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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Marine Glutathione S-Transferases

Marine Biotechnology, 2007
The 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, Xia, Feng, Bal Ram, Singh   +2 more
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Drosophila Glutathione S‐Transferases

2005
The 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 glutathione S-transferases of fish

Fish Physiology and Biochemistry, 1987
Substantial 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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The glutathione peroxidase activity of glutathione S-transferases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
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