The behavior of some chalcones on acetylcholinesterase and carbonic anhydrase activity
Yazarlar (6)
Doç. Dr. Hatice Esra DURAN
Kafkas Üniversitesi, Türkiye
Yeliz Demir
Ardahan Üniversitesi, Türkiye
Muhammet Serhat Özaslan
Ardahan Üniversitesi, Türkiye
Fikret Türkan
Iğdır Üniversitesi, Türkiye
Şükrü Beydemir
Anadolu Üniversitesi, Türkiye
Ömer İrfan Küfrevioğlu
Atatürk Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | DRUG AND CHEMICAL TOXICOLOGY (Q3) | ||
| Dergi ISSN | 0148-0545 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 11-2019 |
| Cilt / Sayı / Sayfa | 42 / 6 / 634–640 | DOI | 10.1080/01480545.2018.1463242 |
| Makale Linki | https://www.tandfonline.com/doi/full/10.1080/01480545.2018.1463242 | ||
| Özet |
| Carbonic anhydrase (CA) has a key role in respiration, carbon dioxide and bicarbonate transport. Acetylcholinesterase (AChE) is a serine hydrolase and mostly abundant at neuromuscular junctions and cholinergic brain synapses. Inhibitors of these enzymes could aid in illuminating the role in disease processes. In this study, we separately purified CA I and CA II from human erythrocytes. The purity of the enzymes was showed by SDS-PAGE analysis. We also investigated the inhibition of seven chalcones toward hCA I, hCA II, and AChE. The chalcones were effective inhibitors of the cytosolic CA isoforms (hCA I and hCA II) and AChE with values in the range of 1.83-7.05 μM for hCA I, 0.59-5.50 μM for hCA II, and 0.61-86.11 μM for AChE. All compounds were showed competitive inhibition aganist both enzymes. These compounds can be a potent inhibitor of AChE enzyme and both cytosolic CA isoenzymes which are commonly used in the pharmaceutical and medical industries. |
| Anahtar Kelimeler |
| Acetylcholinesterase | carbonic anhydrase | chalcone | inhibition | purification |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| WoS | 69 |
| Google Scholar | 89 |