Effect of vitamin E on carbonic anhydrase enzyme activity in rainbow trout (Oncorhynchus mykiss) erythrocytes in vitro and in vivo

Journal of Enzyme Inhibition and Medicinal Chemistry

Gülçın

Özgeriş

et al. 2015

Carbonic anhydrases (CAs, EC 4.2.1.1) had six genetically distinct families described to date in various organisms. There are 16 known CA isoforms in humans. Human CA isoenzymes I and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. Acetylcholine esterase (AChE. EC 3.1.1.7) is a hydrolase that hydrolyzes the neurotransmitter acetylcholine relaying the signal from the nerve. In this study, some trimethoxyindane derivatives were investigated as inhibitors against the cytosolic hCA I and II isoenzymes, and AChE enzyme. Both hCA isozymes were inhibited by trimethoxyindane derivatives in the low nanomolar range. These compounds were good hCA I inhibitors (Kis in the range of 1.66-4.14 nM) and hCA II inhibitors (Kis of 1.37-3.12 nM) and perfect AChE inhibitors (Kis in the range of 1.87-7.53 nM) compared to acetazolamide as CA inhibitor (Ki: 6.76 nM for hCA I and Ki: 5.85 nM for hCA II) and Tacrine as AChE inhibitor (Ki: 7.64 nM).

Section: Methodsmentioning

confidence: 95%

The human carbonic anhydrase isoenzymes I and II (hCA I and II) inhibition effects of trimethoxyindane derivatives

Journal of Enzyme Inhibition and Medicinal Chemistry

Gülçın

Özgeriş

et al. 2015

“…To this end, Sepharose-4B-L-Tyrosine-sulfanilamide affinity chromatography was used for purification of both isoenzymes 71 via a single step described previously [72][73][74] . CA activity determination was realised spectrophotometric method of Verpoorte et al 75 as described previously 76 .…”

Section: Biochemical Studiesmentioning

confidence: 99%

Synthesis of some tetrahydropyrimidine-5-carboxylates, determination of their metal chelating effects and inhibition profiles against acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase

Sujayev

Garibov

Journal of Enzyme Inhibition and Medicinal Chemistry

et al. 2016

107

2-(Methacryloyloxy)ethyl 6-methyl-2-oxo-4-phenyl-1,2,3,4-tetrahydropyrimidine-5-carboxylate, is a cyclic urea derivative synthesized from urea, 2-(methacryloyloxy) ethyl acetoacetate and substituted benzaldehyde, and tested in terms of the inhibition of two physiologically relevant carbonic anhydrase (CA) isozymes I and II. Acetylcholinesterase (AChE) is found in high concentrations in the red blood cells and brain. Butyrylcholinesterase (BChE) is another enzyme abundantly present in the liver and released into blood in a soluble form. Also, they were tested for the inhibition of

“…In this study, both hCA I, and II isoenzymes were purified by Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography [63][64][65] . The affinity chromatography consists Sepharose-4B-L-tyrosine-sulfanilamide that acts as affinity matrix for selective retention of CA isoenzymes [66][67][68] . The column material was prepared according to a previous method 69 .…”

Section: Carbonic Anhydrase I and Ii Isoenzyme Purification And Inhibmentioning

confidence: 99%

Synthesis of diaryl ethers with acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase inhibitory actions

Ozbey

Journal of Enzyme Inhibition and Medicinal Chemistry

Gülçın

et al. 2016

134

A series of diaryl ethers were synthesized and their human (h) carbonic anhydrase (CA) isoenzymes hCA I and II, acetylcholinesterase (AChE), and butyrylcholinesterase (BuChE) inhibitory actions were investigated. The new compounds were synthesized from the corresponding phenols and bromobenzenes via the Ullmann reaction, by using dipicolinic acid as a copper (I) complexing ligand. hCA I and II were inhibited with K i s in the low nanomolar range of 102.01-127.13 nM against hCA I, and of 73.71-113.40 nM against hCA II, whereas the inhibition constants against AChE were of 15.35-18.34 nM and against BChE in the range of 9.07-22.90 nM. The CA inhibition mechanism with these ethers is unknown, but may be similar to that of aryl methyl ethers investigated earlier by computational approaches.