Yazarlar |
Muhammet Serhat Özaslan
Ardahan Üniversitesi, Türkiye |
Yeliz Demir
Ardahan Üniversitesi, Türkiye |
Doç. Dr. Hatice Esra DURAN
Türkiye |
Şükrü Beydemir
Anadolu Üniversitesi, Türkiye |
Ömer İrfan Küfrevioğlu
Atatürk Üniversitesi, Türkiye |
Özet |
Glutathione S-transferases (GSTs) are the superfamily of multifunctional detoxification isoenzymes and play an important role in cellular signaling. In the present study, potential inhibition effects of chalcones were tested against human GST. For this purpose, GST was purified from human erythrocytes with 5.381 EU⋅mg specific activity and 51.95% yield using a GSH-agarose affinity chromatographic method. The effects of chalcones on in vitro GST activity were tested at various concentrations. K constants of chalcones were found in the range of 7.76-41.93 μM. According to the results, 4-fluorochalcone showed a better inhibitory effect compared with the other compounds. The inhibition mechanisms of 2'-hydroxy-4-methoxychalcone and 4-methoxychalcone were noncompetitive, whereas the inhibition mechanisms of 4'- hydroxychalcone, 4- fluorochalcone, and 4,4'- diflurochalcone were competitive. |
Anahtar Kelimeler |
chalcone | glutathione S-transferase | inhibition | purification |
Makale Türü | Özgün Makale |
Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale |
Dergi Adı | JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY |
Dergi ISSN | 1095-6670 |
Dergi Tarandığı Indeksler | SCI-Expanded |
Makale Dili | İngilizce |
Basım Tarihi | 05-2018 |
Cilt No | 32 |
Sayı | 5 |
Doi Numarası | 10.1002/jbt.22047 |
Makale Linki | http://doi.wiley.com/10.1002/jbt.22047 |
Atıf Sayıları | |
WoS | 52 |
Google Scholar | 66 |