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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 K 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.

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.

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