Effect of Pharmaceutical Potential Endocrine Disruptor Compounds on Protein Disulfide Isomerase Reductase Activity Using Di-Eosin-Oxidized-Glutathion
Figure 1
PDI-catalyzed reduction of di-eosin oxidized-glutathion (DiE-GSSG) in the absence or presence of increasing concentrations of ethynylestradiol (EE2).
A/ Kinetics of PDI-catalyzed reduction of DiE-GSSG in the absence or presence of increasing concentrations of ethynylestradiol (EE2). PDI activity is determined using initial velocity of the reaction as measured through the abolishment of fluorescence self quenching in 2.4 µM DiE-GSSG when it is reduced into two molecules of E-GSH in the presence of 33 µM DTeT. B/ Comparison of Kinetics of PDI-catalyzed reduction of DiE-GSSG as in A/ in the absence (○) or presence (•) of 10% (v/v) ethanol in the 100 mM phosphate buffer pH 8.0.