Makale detayı · 2018 · article
Purification of glutathione S-transferase enzyme from quail liver tissue and inhibition effects of (3a iR/i ,4 iS/i ,7 iR/i ,7a iS/i )-2-(4-(( iE/i )-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1 iH/i -4,7-methanoisoindole-1,3(2 iH/i )-dione derivatives on the enzyme activity/title
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- YÖKSİSYÖKSİS makale kaydı
- YÖKSİS dergi adıJournal of Biochemical and Molecular Toxicology
- Katalog eşleşmesi (ISSN)Journal of Biochemical and Molecular Toxicology
- OpenAlexOpenAlex zenginleştirmesi (özet, atıf, konular)
- Semantic Scholaratıf sayısı (OpenAlex ile birleştirilmez)
Özet
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 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.
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