Akademik Veri Yönetim Sistemi
Drug and Chemical Toxicology, cilt.42, ss.634-640, 2019 (SCI-Expanded)
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 lM for hCA I, 0.59–5.50 lM for
hCA II, and 0.61–86.11 lM 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.