| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY (Q4) | ||
| Dergi ISSN | 1095-6670 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 03-2018 |
| Cilt / Sayı / Sayfa | 32 / 3 / 22034–0 | DOI | 10.1002/jbt.22034 |
| Makale Linki | http://doi.wiley.com/10.1002/jbt.22034 | ||
| Özet |
| 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 … |
| Anahtar Kelimeler |
| GST | Quail liver | enzyme purification | inhibition | methanoisoindole |
| Atıf Sayıları | |
| Google Scholar | 34 |
| Web of Science | 20 |
| Dergi Adı | JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY |
| Yayıncı | John Wiley & Sons Inc. |
| Açık Erişim | Hayır |
| ISSN | 1095-6670 |
| E-ISSN | 1099-0461 |
| CiteScore | 6,0 |
| SJR | 0,772 |
| SNIP | 0,725 |