Glutathione S-transferase subunits

H19. Hayes, J. D., Judah, D. J., McLellan, L. I., Kerr, L. A., Peacock, S. D., and Neal, G. E., Ethoxyquin-induced resistance to aflatoxin Bj in the rat is associated with the expression of a novel Alpha-class glutathione S-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin 8,-8,9-epoxide. Biochem. J. 279, 385-398 (1991). 

H63. Hussey, A. J., Stockman, P. K., Beckett, G. J., and Hayes, J. D., Variations in the glutathione S-transferase subunits expressed in human livers. Biochim. Biophys. Acta 874, 1-12 (1986). 

Igarashi, T., Tsuchiya, T., Shikata, Y., Sagami, F., Tagaya, O., Horie, T., and Satoh, T., Developmental aspects of a unique glutathione S-transferase subunit Yx in the liver cytosol from rats with hereditary hyperbilimbinuria. Comparison with rat fetal liver transferase subunit Y fetus. Biochem. J. 283, 307-311 (1992). 

Maheo K, Antras-Eerry J, Morel E, Langouet S, Guillouzo A. Modulation of glutathione S-transferase subunits A2, Ml, and PI expression by interleukin-1 p in rat hepatocytes in primary culture. J Biol Chem 1997 272 16125-16132. 

Treptow-van Lishaut, S., Rechkemmer, G., Rowland, L, Dolara, P., and Pool-Zobel, B.L., The carbohydrate crystalean and colonic microflora modulate expression of glutathione S-transferase subunits in colon of rats, Eur. J. Nutr., 38, 76-83, 1999. 

It should be emphasized that the nature of all presented protocols is very general and, thus, their application for a comprehensive characterization of your favorite multiprotein complex (YFMPC) in yeast might require only minor modifications. The logical sequence of all required steps is schematically shown in Fig. 2.1. The initial large-scale Ni affinity isolation of eIF3 followed by mass spectrometry (MS) of its subunit composition has already been described (Asano et al, 2002), and methods for identification of protein-protein interactions such as yeast two-hybrid (Y2H) and in vitro glutathione-S-transferase (GST) pull-down analysis are presented in volume 429. This chapter focuses on a description of the small-scale one-step in vivo affinity purification techniques that were used to determine the effects of deletions and... 

Fung and colleagues examined the metabolic conversion of organic nitrates in sub-cellular fractions of bovine coronary artery smooth muscle cells [66, 67]. They found NO-generating capacity to be present in membrane fractions and, with the use of marker enzymes, identified plasma membrane as the primary location. The enzyme involved in bioconversion was not glutathione-S-transferase [68] and differed from those that catalyse activation of organic nitrites [69]. Partial purification [70] established that the molecular sizes of the native enzyme and subunits were approximately 200 kDa and 58 kDa respectively, and that enzymic activity depends on the presence of a free thiol group. 

Rushmore, T.H. and Pickett, C.B. (1990) Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. Journal of Biological Chemistry, 265, 14648-14653. 

Cydophilin A Ferritin light subunit GAPDH Galectin-1 Glutathione S-transferase MnSOD Protein disulfide isomerase A3 precursor... 

Friling RS, Bergelson S, Daniel V. 1992. Two adjacent AP-l-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene. Proc Natl Acad Sci USA 89 668-672. 

Nguyen T, Rushmore TH, Pickett CB. 1994. Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-0-tetradecanoylphorbol-13-acetate. J Biol Chem 269 13656-13662. 

S. Liu and C. B. Pickett. The rat liver glutathione S-transferase Ya subunit gene Character of the binding properties of a nuclear protein from Hep G2 cells that have affinity for the antioxidant response element. Biochemistry, 35 (35), 11517—11521, 1996. 

Rushmore TH, King RG, Paulson KE, Pickett CB. 1990. Regulation of glutathione S-transferase Ya subunit gene expression identification of a unique xenobiotic responsive element controlling inducible expression by planar aromatic... 

Friling RS, Bensimon A, Tichauer Y, Daniel V. 1990. Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element. Proc. Natl. Acad. Sci. USA 87 6258-62... 

Telakowski-Hopkins, C.A., R.G. King and C.B. Pickett. Glutathione S-transferase Ya subunit gene identification of regulatory elements required for basal level and inducible expression. Proc. Natl Acad. Sci. USA 85 1000-1004, 1988. 

D2. DeJong, J. L., Chang, C. M Whang-Peng, J., Knutsen, T., and Tu, C. P. D., The human liver glutathione S-transferase gene superfamily Expression and chromosome mapping of an Hj, subunit cDNA. Nucleic Acids Res. 16, 8541-8554 (1988). 

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