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The behavior of some chalcones on acetylcholinesterase and carbonic anhydrase activity      
Yazarlar
Doç. Dr. Hatice Esra DURAN Doç. Dr. Hatice Esra DURAN
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
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
Makale Türü Özgün Makale
Makale Alt Türü SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale
Dergi Adı DRUG AND CHEMICAL TOXICOLOGY
Dergi ISSN 0148-0545
Dergi Tarandığı Indeksler SCI-Expanded
Dergi Grubu Q3
Makale Dili İngilizce
Basım Tarihi 11-2019
Cilt No 42
Sayı 6
Sayfalar 634 / 640
Doi Numarası 10.1080/01480545.2018.1463242
Makale Linki https://www.tandfonline.com/doi/full/10.1080/01480545.2018.1463242