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Glutathione-S-transferase theta

Kelsey, K.T., Wiencke, J.K., Ward, J., Bechtold, W. Fajen, J. (1995) Sister-chromatid exchanges, glutathione S-transferase theta deletion and cytogenetic sensitivity to diepoxybutane in lymphocytes from butadiene monomer production workers. Mutat. Res., 335, 267-273... [Pg.211]

Wiencke, J.K., Pemble, S., Ketterer, B. Kelsey, K.T. (1995) Gene deletion of glutathione S-transferase theta correlation with induced genetic damage and potential role in endogenous mutagenesis. Cancer Epidem. Biomarkers Prev., 4, 253-259... [Pg.224]

Pemble, S., Schroeder, K.R., Spencer, S.R., Meyer, D.J., Hallier, E., Bolt, H.M., Ketterer, B. Taylor, J.B. (1994) Human glutathione S-transferases theta (GSTTI) cDNA cloning and the characterization of a genetic polymorphism. Biochem. J., 300, 271-276... [Pg.309]

Glutathione S-transferase theta I was localised in type II pneumocytes of the mouse (Quondamat-TEO et al. 1998). [Pg.206]

Leaver, M.J., Scott, K., George, S.G. (1993). Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice Pleuronectes platessa), with structural similarities to plant, insect and mammalian theta-class coenzymes. Journal of Biochemistry, 292 189-195. [Pg.131]

Mainwaring, G.W., Foster, J.R. Green, T. (1998) Nuclear and cellular immunolocalization of theta class glutathione S-transferase GSTTl-1 in the liver and lung of the mouse. Biochem. J., 329, 431-432... [Pg.307]

Sherratt, P.J., Pulford, D.J., Harrison, D.J., Green, T. Hayes, J.D. (1997) Evidence that human class theta glutathione S-transferases Tl-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GST Tl-1 with that of classes alpha, mu and pi GST in human. Biochem. J., 326. 837-846... [Pg.312]

H59. Hussey, A. J., and Hayes, J. D., Characterization of a human class theta glutathione S-transferase with activity towards 1-menaphthyl sulphate. Biochem. J. 286, 929-935 (1992). [Pg.369]

The glutathione transferases are soluble dimeric proteins that are composed of identical subunits, although some forms are heterodimers. These enzymes are present in most tissues and are primarily cytosolic (approximately 95%), although a small percentage are found in the endoplasmic reticulum (approximately 5%). The cytosolic glutathione S-transferases (GSTs) are divided into six families or classes alpha, kappa, mu, pi, sigma, and theta. The alpha, mu, and pi GST classes are primarily responsible for most of the catalytic activity associated with liver detoxication of xenobiotics. [Pg.129]

P6. Pemble, S. E., and Taylor, J. B., An evolutionary perspective on glutathione transferases inferred flom class theta cDNA sequences. Biochem. J. 287, 957-963. [Pg.374]


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