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Research Article

Potentiation of the reductase activity of protein disulphide isomerase (PDI) by 19-nortestosterone, bacitracin, fluoxetine, and ammonium sulphate

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Pages 681-687 | Received 30 Jul 2010, Accepted 07 Dec 2010, Published online: 21 Jan 2011

Figures & data

Figure 1.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence of various concentrations (0–10−4 M) of melatonin, auxin, serotonin or metoprolol.

Figure 1.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence of various concentrations (0–10−4 M) of melatonin, auxin, serotonin or metoprolol.

Figure 2.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence of various concentrations (0–10−4 M) of bisphenol A. BPA, bisphenol A; RFU, relative fluorescence unit.

Figure 2.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence of various concentrations (0–10−4 M) of bisphenol A. BPA, bisphenol A; RFU, relative fluorescence unit.

Figure 3.  Effect of increasing concentrations of bacitracin (BAC) on protein disulphide isomerase (PDI) reductase activity. Left panel: kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by PDI in the presence of various concentrations (0–10−4 M) of BAC. Right panel: initial velocity of PDI reducing activity as a function of BAC concentration relative to the velocity in the absence of bacitracin taken as control (n = 3). RFU, relative fluorescence unit.

Figure 3.  Effect of increasing concentrations of bacitracin (BAC) on protein disulphide isomerase (PDI) reductase activity. Left panel: kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by PDI in the presence of various concentrations (0–10−4 M) of BAC. Right panel: initial velocity of PDI reducing activity as a function of BAC concentration relative to the velocity in the absence of bacitracin taken as control (n = 3). RFU, relative fluorescence unit.

Figure 4.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence of various concentrations (0, 10−4, 10−3 M) of fluoxetine (FLX). The figure also shows the effect of 10% ethanol alone as also present with 10−3 M FLX.

Figure 4.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence of various concentrations (0, 10−4, 10−3 M) of fluoxetine (FLX). The figure also shows the effect of 10% ethanol alone as also present with 10−3 M FLX.

Figure 5.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence or absence of 0.5 M ammonium sulphate. RFU, relative fluorescence unit.

Figure 5.  Kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by protein disulphide isomerase in the presence or absence of 0.5 M ammonium sulphate. RFU, relative fluorescence unit.

Figure 6.  Inhibition of protein disulphide isomerase (PDI) reductase activity by diethylstilbestrol (DES) in the presence of a potentiating concentration of 19-nortestosterone (19-NT). Left panel: kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by PDI in the presence of 10−5 M of either DES or 19-NT or in the presence of 10−5 M 19-NT together with various concentrations (10−9, 10−7, 10−5 M) of DES. Right panel: initial velocity of PDI reducing activity in the presence of either DES or 19-NT alone or in combination (data from left panel). RFU, relative fluorescence unit.

Figure 6.  Inhibition of protein disulphide isomerase (PDI) reductase activity by diethylstilbestrol (DES) in the presence of a potentiating concentration of 19-nortestosterone (19-NT). Left panel: kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by PDI in the presence of 10−5 M of either DES or 19-NT or in the presence of 10−5 M 19-NT together with various concentrations (10−9, 10−7, 10−5 M) of DES. Right panel: initial velocity of PDI reducing activity in the presence of either DES or 19-NT alone or in combination (data from left panel). RFU, relative fluorescence unit.

Figure 7.  Inhibition of protein disulphide isomerase (PDI) reductase activity by ethynylestradiol (EE2) in the presence of a potentiating concentration of fluoxetine (FLX). Left panel: kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by PDI in the presence of 10−3 M FLX or 10−5 or 10−4 M EE2 alone or in the presence of 10−3 M FLX. Right panel: initial velocity of PDI reducing activity in the presence of either FLX or EE2 alone or in combination. RFU, relative fluorescence unit.

Figure 7.  Inhibition of protein disulphide isomerase (PDI) reductase activity by ethynylestradiol (EE2) in the presence of a potentiating concentration of fluoxetine (FLX). Left panel: kinetics of di-eosin oxidized glutathione reduction into fluorescent E-GSH catalyzed by PDI in the presence of 10−3 M FLX or 10−5 or 10−4 M EE2 alone or in the presence of 10−3 M FLX. Right panel: initial velocity of PDI reducing activity in the presence of either FLX or EE2 alone or in combination. RFU, relative fluorescence unit.

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