scholarly journals Inhibitory effect of novel pyrazole carboxamide derivatives on human carbonic anhydrase enzyme

2012 ◽  
Vol 28 (2) ◽  
pp. 328-336 ◽  
Author(s):  
Elvan Şen ◽  
Zuhal Alım ◽  
Hatice Duran ◽  
Mehmet Mustafa İşgör ◽  
Şükrü Beydemir ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Inhibitory Effect ◽  
Human Carbonic Anhydrase ◽  
Carbonic Anhydrase Enzyme

Calcium transport across avian uterus. III. Comparison of laying and nonlaying birds.

1977 ◽  
Vol 232 (4) ◽  
pp. E437 ◽  
Author(s):  
T W Pearson ◽  
T J Pryor ◽  
A M Goldner
Keyword(s):  
Enzyme Activity ◽  
Carbonic Anhydrase ◽  
Calcium Transport ◽  
Statistical Difference ◽  
Inhibitory Effect ◽  
Calcium Fluxes ◽  
Laying Quail ◽  
Presence And Absence ◽  
Carbonic Anhydrase Enzyme ◽  
Calcium Secretion

Transepithelial calcium fluxes were measured across isolated uterus of laying, nonlaying, and molting quail under conditions where no electrochemical difference existed across the tissue. Net uterine transfer of calcium in molting and nonlaying birds occurs in the secretory direction and is approximately one-fifth the value obtained for laying birds. The carbonic anhydrase enzyme activity of uteri from laying birds is twice that of uteri from molting birds and five times greater than that of uteri from nonlaying birds. When measured in the presence and absence of 2-mercaptoethanol or dithiothreitol, no statistical difference exists in uterine carbonic anhydrase activities of laying birds or the inhibitory effect of acetazolamide. These results indicate that nonlaying and molting quail secrete calcium at a rate much lower than that of laying quail and that net uterine transfer of calcium exhibits varing degrees of dependence on bicarbonate ion in laying, nonlaying, and molting birds. Carbonic anhydrase data sugges that the activtiy of this enzyme in the quail uterus may be related to uterine calcium secretion.

scholarly journals Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

2016 ◽  
Author(s):  
Hayriye Genç ◽  
Ramazan Kalin ◽  
Zeynep Köksal ◽  
Nastaran Sadeghian ◽  
Umit M. Kocyigit ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Acetylcholinesterase Inhibitors ◽  
Inhibitory Effect ◽  
Beta Lactam ◽  
Beta Lactams ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

β-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. β-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was also examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The results reveal that β-lactams are inhibitors of hCA I, II and AChE. The Ki values of β-lactams (2a-k) were 0.44-6.29 nM against hCA I, 0.93-8.34 nM against hCA II, and 0.25-1.13 nM against AChE. Our findings indicate that β-lactams (2a-k) inhibit both CA isoenzymes and AChE at low nanomolar concentrations.

In-Silico Analysis of Chromone Containing Sulfonamide Derivatives as Human Carbonic Anhydrase Inhibitors

2013 ◽  
Vol 9 (4) ◽  
pp. 608-616 ◽  
Author(s):  
Zaheer Ul-Haq ◽  
Saman Usmani ◽  
Uzma Mahmood ◽  
Mariya al-Rashida ◽  
Ghulam Abbas
Keyword(s):  
Carbonic Anhydrase ◽  
In Silico ◽  
In Silico Analysis ◽  
Carbonic Anhydrase Inhibitors ◽  
Human Carbonic Anhydrase ◽  
Silico Analysis
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