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Sulfonamide-bearing thiazole compounds were synthesized and their inhibitory effects on the activity of purified human carbonic anhydrase I and II were evaluated. Human carbonic anhydrase isoenzymes (hCA-I and hCA-II) were purified from erythrocyte cells by affinity chromatography. The inhibitory effects of the 12 synthesized sulfonamide (5a–l) on the hydratase and esterase activities of these isoenzymes (hCA-I and hCA-II) were studiedin vitro. In relation to these activities, the inhibition equilibrium constants (Ki) were determined. The results showed that all the synthesized compounds inhibited the CA isoenzyme activity. Among them5bwas found to be the most active (IC50 = 0.35 μM;Ki: 0.33 μM) for hCA I and hCA II. [ABSTRACT FROM PUBLISHER]

Synthesis of carbazole substituted chalcone urea derivatives and their polyphenol oxidase enzyme activity effects on the diphenolase activity of banana tyrosinase were evaluated. Tyrosinase has been purified from banana on an affinity gel comprised of Sepharose 4B- l-tyrosine-p-aminobenzoic acid. The results showed that most of the compounds ( 3,4,5a,5d-h) inhibited and some of them ( 5c,5i-l) activated the tyrosinase enzyme activity. The molecular calculations were performed using Gaussian software for the synthesized compounds to explain the experimental results. [ABSTRACT FROM AUTHOR]

A newly series of water-soluble 1-alkyl-3-(4-methyl-7, 8-dihydroxy-2H-chromen-2-one) benzimidazolium chloride salts (3a-j) were synthesized and their inhibitory effects on the activity of purified human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II from human erythrocytes were purified by a simple one step procedure by using Sepharose 4B-L-tyrosine-sulphanilamide affinity column. The result showed that all the synthesized compounds were inhibited the CA isoenzymes activity. Among them, 3g and 3j were found to be most active (IC50 = 22.09 μM and 20.33 μM) for hCA I and hCA II, respectively. [ABSTRACT FROM AUTHOR]

The in vitro effects of the anabolic compounds, zeranol, 17 β-estradiol, diethylstilbestrol (DES), and trenbolone, on the activity of purified human carbonic anhydrase I and II were evaluated. In vitro CA enzyme activity was determined colorimetrically using the CO2 hydration method of Maren. IC50 values of the compounds that caused inhibition were determined by means of activity percentage diagrams. The IC50 concentrations of zeranol, 17 β-estradiol, DES and trenbolone on hCA I were 94, 55, 10, 898 µM and for hCA II 89, 159, 439 and 101 μM, respectively. [ABSTRACT FROM AUTHOR]