Glutathione S-Transferases GST

Figure 7-12. Use of glutathione S-transferase (GST) fusion proteins to purify recombinant proteins. (GSH, glutathione.)...

The common mechanisms of drug resistance in ovarian cancer include (1) alteration of drug inactivation by agents such as glutathione-S-transferase (GST), (2) enhanced DNA repair,... 

The potential of coupling SPR with mass spectrometry has been demonstrated using glutathione-S-transferase (GST) and an anti-GST... 

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... 

The glutathione S-transferases (GST) enzymes are dimeric enzymes that catalyze the conjugation of glutathione (GSH) to electrophilic xenobiotics in order to inactivate them and facilitate their... 

The intracellular nucleophile glutathione (GSH y-Glu-Cys-Gly) acts as a protective mechanism against electrophilic insults and may be present at concentrations of up to 10 mM [26]. The reaction of glutathione with a non-polar compound bearing an electrophilic carbon, nitrogen or sulfur atom may be mediated enzymatically by glutathione-S-transferase (GST), with typical substrates being species such as arene oxides, quinones and a,P-unsaturated carbonyl compounds. 

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