Results 141 to 150 of about 46,208 (193)

Glutathione Transferases and Cancer

Critical Reviews in Biochemistry and Molecular Biology, 1992
The glutathione transferases, a family of multifunctional proteins, catalyze the glutathione conjugation reaction with electrophilic compounds biotransformed from xenobiotics, including carcinogens. In preneoplastic cells as well as neoplastic cells, specific molecular forms of glutathione transferase are known to be expressed and have been known to ...
S, Tsuchida, K, Sato
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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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Insect glutathione transferases

Drug Metabolism Reviews, 2011
This article is an overview of the current knowledge of insect glutathione transferases. Three major topics are discussed: the glutathione transferase contributions to insecticide resistance, the polymorphic nature of the insect glutathione transferase superfamily, and a summary of the current structure-function studies on insect glutathione ...
Albert J, Ketterman, Chonticha, Saisawang, Jantana, Wongsantichon   +2 more
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Mosquito Glutathione Transferases

2005
The glutathione transferases (glutathione S-transferases, GSTs) are a diverse family of enzymes involved in a wide range of biological processes, many of which involve the conjugation of the tripeptide glutathione to an electrophilic substrate. Relatively little is known about the endogenous substrates of mosquito GSTs, and most studies have focused on
Hilary, Ranson, Janet, Hemingway
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Measurement of Glutathione Transferases

Current Protocols in Toxicology, 2002
AbstractThere are multiple glutathione transferase genes, the proteins for which have different substrate specificities. The various genes are differentially expressed such that species and organs and tissues differ qualitatively and quantitatively for cytosolic and membrane‐bound forms. This unit provides protocols for analysis of transferase activity
B, Mannervik, P, Jemth
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Sigma-class glutathione transferases

Drug Metabolism Reviews, 2011
Mammalian cytosolic glutathione transferases (GSTs) can be grouped into seven classes. Of these, the sigma class is also widely distributed in nature, with isoforms found in both vertebrates and invertebrates. It contains examples of proteins that have evolved specialized functions, such as the cephalopod lens S-crystallins, the mammalian hematopoietic
Flanagan, Jack U., Smythe, Mark L.
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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 transferase

2000
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate.
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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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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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