Abstract
Inhibitors of carbonic anhydrase (CA) have been carried out in many therapeutic applications, especially antiglaucoma activity. In this study, we investigated some uracil derivatives (4–12) to inhibit human CA I (hCA I) and II (hCA II) isoenzymes. The KI values of the compounds 4–12 are in the range of 0.085–428 µM for hCA I and of 0.1715–645 µM against hCA II, respectively. It is concluded from the kinetic investigations, all compounds used in the study act as competitive inhibitors with substrate, 4-NPA. Uracil derivatives are emerging agents for the inhibiton of carbonic anhydrase which could be used in biomedicine.
Highlights
Uracil, one of the pyrimidine bases, is commonly present in ribonucleic acid (RNA)[1]
Some of these human carbonic anhydrase (CA) isoenzymes such as CA I, II, III, VII and XIII are cytosolic, some forms, CA IV, IX, XII and XIV, are membrane bound, two ones as CA VA and VB are mitochondrial and CA VI is found in saliva
The human carbonic anhydrase isozymes were eluted with 1 M NaCl/25 mM Na2HPO4 and 0.1 M CH3COONa/0.5 M NaClO4, respectively
Summary
To cite this article: Emir Alper Türkoğlu, Murat Şentürk, Claudiu T. View related articles View Crossmark data Citing articles: 19 View citing articles. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2017 VOL.
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