The behavior of some chalcones on acetylcholinesterase and carbonic anhydrase activity
 
Yazarlar (6)
Doç. Dr. Hatice Esra DURAN Kafkas Üniversitesi, Türkiye
Prof. Dr. Yeliz Demir Ardahan Üniversitesi, Türkiye
Doç. Dr. Muhammet Serhat Özaslan Ardahan Üniversitesi, Türkiye
Doç. Dr. Fikret Türkan Iğdır Üniversitesi, Türkiye
Prof. Dr. Şükrü Beydemir Anadolu Üniversitesi, Türkiye
Prof. Dr. 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 (Q2)
Dergi ISSN 0148-0545 Dergi Bilgileri (2019)
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 11-2019
Kabul Tarihi 06-04-2018 Yayınlanma Tarihi 04-06-2018
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
UAK Araştırma Alanları
Tıbbi Biyokimya
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 Ki 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 …
Anahtar Kelimeler
Acetylcholinesterase | carbonic anhydrase | chalcone | inhibition | purification
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
Web of Science 70
Google Scholar 89
The behavior of some chalcones on acetylcholinesterase and carbonic anhydrase activity

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