Purification of glutathione S-transferase enzyme from quail liver tissue and inhibition effects of (3aR,4S,7R,7aS)-2-(4-((E)-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione derivatives on the enzyme activity.

The use of quail meat and eggs has made this animal important in recent years, with its low cost and high yields. Glutathione S-transferases (GST, E.C.2.5.1.18) are an important enzyme family, which play a critical role in detoxification system. In our study, GST was purified from quail liver tissue with 47.88-fold purification and 12.33% recovery by glutathione agarose affinity chromatography. The purity of enzyme was checked by SDS-PAGE method and showed a single band. In addition, inhibition effects of (3aR,4S,7R,7aS)-2-(4-((E)-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1H-4,7methanoisoindole-1,3(2H)-dion derivatives (1a-g) were investigated on the enzyme activity. The inhibition parameters (IC50 and Ki values) were calculated for these compounds. IC50 values of these derivatives (1a-e) were found as 23.00, 15.75, 115.50, 10.00, and 28.75 µM, respectively. Ki values of these derivatives (1a-e) were calculated in the range of 3.04 ± 0.50 to 131.50 ± 32.50 µM. However, for f and g compounds, the inhibition effects on the enzyme were not found.

The Effect of Mercury Chloride and Boric Acid on Rat Erythrocyte Enzymes.

The aim of this study was to investigate the effects of mercury chloride and boric acid on rat (Wistar albino) erythrocyte: glucose 6-phosphate dehydrogenase (G6PD), 6-phosphoglucona-te dehydrogenase (6PGD), thioredoxin reductase (TrxR), glutathione reductase (GR) and glutathione S-transferase (GST) enzymes in vivo, and the rat erythrocyte G6PD enzyme in vitro. In the in vivo study, 24 male rats were divated into three different groups: control (C), mercury chloride (M), and mercury chloride + boric acid (M + BA). At the completion of this study, a significant degree of inhibition for both G6PD and GST enzyme activity was observed in the M groups when compared to the C group (p < 0.05), and no significant effect was observed in the 6PGD enzyme. However, there was significantly increased TrxR and GR enzyme activity of both the M and M + BA groups (p < 0.05). In the in vitro study, the G6PD enzyme from rat erythrocytes was purified with 2',5'-ADP Sepharose-4B affinity chromatography, and the effect of both mercury chloride and boric acid on the enzyme activity was investigated. The results showed that boric acid increased the G6PD enzyme activity while the mercury ions that inhibited the enzyme activity (IC50 values of 346 µM and Ki values of 387 µM) were noncompetitive.