Heavy metal ion inhibition studies of human, sheep and fish α-carbonic anhydrases

Demirdağ, Ramazan; Yerlikaya, Emrah; Şentürk, Murat; Küfrevioğlu, Ömer İrfan; Supuran, Claudiu T.

doi:10.3109/14756366.2011.640633

Cited by 39 publications

(13 citation statements)

References 45 publications

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“…CA isozymes are involved in the pH homeostasis, ion transport, water and electrolyte balance, bone resorption, calcification, and tumorigenesis . In a recent preliminary work from our group, we investigated the interaction between natural phenolic compounds, amino acid sulfonamide derivatives, hydroxy/methoxy organic compounds, and some nitroaromatic compounds with two cytosolic catalytically active isoforms (CA I and II) of the metalloenzyme CA .…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Biological Evaluation of Novel Bischalcone Derivatives as Carbonic Anhydrase Inhibitors

Arslan

Çelik

Celik

et al. 2016

Archiv der Pharmazie

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Design and synthesis of a new type of bischalcones as an alternative to natural and synthetic bischalcones are reported for the first time. Key steps involved the solvent-free Claisen-Schmidt condensation of chalcones, and the successful first application of the diazotization-diazocoupling reaction in the synthesis of CNNC-linked bischalcones by simple structural modification of p-aminoacetophenone. The structures of all compounds were confirmed by means of FT-IR, (1) H and (13) C NMR, ESI/MS, and elemental analysis. In addition, the newly synthesized compounds were screened for carbonic anhydrase inhibition activities. Almost all bischalcones exhibited moderate-to-good inhibitory activities.

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Section: Introductionmentioning

confidence: 99%

Synthesis and Biological Evaluation of Novel Bischalcone Derivatives as Carbonic Anhydrase Inhibitors

Arslan

Çelik

Celik

et al. 2016

Archiv der Pharmazie

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“…Similar results have been observed for the enzyme from different sources. For example, human erythrocyte CA is 29 kDa, bovine erythrocyte CA is 29 kDa and European seabass liver CA is 30.2 kDa [3][4][5][6] . In addition to establishment of molecular weight of the enzyme, Rf values were calculated for the enzyme and standard proteins, and Rf-LogMW graph was obtained according to Laemmli' method.…”

Section: Resultsmentioning

confidence: 99%

“…After the package of red cells was washed with KC1 solution (0.16 M) three times, the samples were centrifuged at 2500 Â g each time and supernatants were removed. The erythrocytes were hemolyzed with five volumes of ice-cold water and centrifuged (þ4 C, 10 000Â g) for 30 min to remove the ghosts and intact cells 6 .…”

Section: Preparation Of the Hemolysatementioning

confidence: 99%

“…Some of them are cytosolic (CA I, CA II, CA III, CA VII and CA XIII), others are membrane bound (CA IV, CA IX, CA XII and CA XIV), two are mitochondrial (CA VA and CA VB), and one is secreted in saliva (CA VI). It has been reported that CA XV isoform is not expressed in humans or in other primates, but it is abundant in rodents and other vertebrates 1,[3][4][5][6][7] . CAs are produced in a variety of tissues where they participate in several important biological processes such as acid-base balance, respiration, carbon dioxide and ion transport, bone resorption, ureagenesis, gluconeogenesis, lipogenesis and body fluid generation 1,[4][5][6] .…”

Section: Introductionmentioning

confidence: 99%

“…CAs are produced in a variety of tissues where they participate in several important biological processes such as acid-base balance, respiration, carbon dioxide and ion transport, bone resorption, ureagenesis, gluconeogenesis, lipogenesis and body fluid generation 1,[4][5][6] . Up to now, CA has been purified from many different tissues including human erythrocytes [8][9][10] , fish liver 5 , fish erythrocytes 6 , rainbow trout gill and liver 6,11 , similarly some chemicals and metal ions inhibition effects on human and rainbow trout enzymes are investigated [4][5][6][7][8][9][10][11][12][13][14] . Gerze chicken, also known as Hacı Kadı, is the one of two endemic chicken breeds of Turkey.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of carbonic anhydrase from Turkish native “Gerze” chicken and influences of metal ions on enzyme activity

Mercan

Ekinci

Supuran

2014

Journal of Enzyme Inhibition and Medicinal Chemistry

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Carbonic anhydrase was purified and characterized from erythrocytes of the Turkish native chicken, Gerze, for the first time. The enzyme was purified 57.65-fold with a yield of 52%, and a specific activity of 954.08 U/mg proteins having optimum pH at 8.0; optimum temperature at 30 C; optimum ionic strength at 10 mM and stable pH at 8.0. showed weaker actions. All tested metals inhibited the enzyme in competitive manner. Our findings indicate that these metals inhibit the chicken enzyme in a similar manner to other a-CAs from mammals investigated earlier, but susceptibility to various metals differ between the native chicken and other mammalian enzymes.

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Catalytic Mechanism of α-Class Carbonic Anhydrases: CO2 Hydration and Proton Transfer

Boone

Pinard

McKenna

et al. 2013

Subcellular Biochemistry

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The carbonic anhydrases (CAs; EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible hydration of carbon dioxide (CO2) and dehydration of bicarbonate (HCO3 (-)) in a two-step ping-pong mechanism: [Formula: see text] CAs are ubiquitous enzymes and are categorized into five distinct classes (α, β, γ, δ and ζ). The α-class is found primarily in vertebrates (and the only class of CA in mammals), β is observed in higher plants and some prokaryotes, γ is present only in archaebacteria whereas the δ and ζ classes have only been observed in diatoms.The focus of this chapter is on α-CAs as the structure-function relationship is best understood for this class, in particular for humans. The reader is referred to other reviews for an overview of the structure and catalytic mechanism of the other CA classes. The overall catalytic site structure and geometry of α-CAs are described in the first section of this chapter followed by the kinetic studies, binding of CO2, and the proton shuttle network.

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Heavy metal ion inhibition studies of human, sheep and fish α-carbonic anhydrases

Cited by 39 publications

References 45 publications

Synthesis and Biological Evaluation of Novel Bischalcone Derivatives as Carbonic Anhydrase Inhibitors

Synthesis and Biological Evaluation of Novel Bischalcone Derivatives as Carbonic Anhydrase Inhibitors

Characterization of carbonic anhydrase from Turkish native “Gerze” chicken and influences of metal ions on enzyme activity

Catalytic Mechanism of α-Class Carbonic Anhydrases: CO2 Hydration and Proton Transfer

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