Purification of glutathione S‐transferase enzyme from quail liver tissue and inhibition effects of (3a<i>R</i>,4<i>S</i>,7<i>R</i>,7a<i>S</i>)‐2‐(4‐((<i>E</i>)‐3‐(aryl)acryloyl)phenyl)‐3a,4,7,7a‐tetrahydro‐1<i>H</i>‐4,7‐methanoisoindole‐1,3(2<i>H</i>)‐dione derivatives on the enzyme activity

Abstract

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 K_i 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. K_i 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.