| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale |
| Dergi Adı | JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY |
| Dergi ISSN | 1095-6670 Wos Dergi Scopus Dergi |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q4 |
| Makale Dili | İngilizce |
| Basım Tarihi | 03-2018 |
| Cilt No | 32 |
| Sayı | 3 |
| Sayfalar | 22034 / 0 |
| DOI Numarası | 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 (IC and K values) were calculated for these compounds. IC values of these derivatives (1a-e) were found as 23.00, 15.75, 115.50, 10.00, and 28.75 μM, respectively. K 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. |
| Anahtar Kelimeler |
| GST | Quail liver | enzyme purification | inhibition | methanoisoindole |
| Atıf Sayıları | |
| WoS | 20 |
| Google Scholar | 33 |
| 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 |