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Measurement of Glutathione Transferases
Current Protocols in Toxicology, 2002AbstractThere 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, 2011Mammalian 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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Glutathione Transferases and Cancer
Critical Reviews in Biochemistry and Molecular Biology, 1992The 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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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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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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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, 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 Transferases and Carcinogenesis
1986Carcinogenesis has been regarded as being divisible into at least 3 major phases: (a) initiation, a largely irreversible process which has been compared to mutation; (b) promotion, a process during which cells undergo phenotypic changes, some of which are referred to as preneoplastic, and a proportion of which attain autonomy when they can be regarded ...
B, Ketterer +4 more
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Mammalian Cytosolic Glutathione Transferases
Current Protein & Peptide Science, 2008Glutathione Transferases (GSTs) are crucial enzymes in the cell detoxification process catalyzing the nucleophilic attack of glutathione (GSH) on toxic electrophilic substrates and producing a less dangerous compound. GSTs studies are of great importance since they have been implicated in the development of drug resistance in tumoral cells and are ...
Daniel F A R, Dourado +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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