Inhibitory properties of some heavy metals on carbonic anhydrase I and II isozymes activities purified from Van Lake fish (Chalcalburnus Tarichi) gill

  • Müslüm Kuzu
  • Veysel Çomaklı
  • Ebru Akkemik
  • Mehmet Çiftci
  • Ömer İrfan Küfrevioğlu
Article

Abstract

In this study, CA I and II isoenzymes were purified from Van Lake fish gills by using Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography and to determine the effects of some metals on the enzyme activities. For purified CA I isoenzyme, yield, specific activity, and purification fold were obtained as 42.07%, 4948.12 EU/mg protein, and 116.61 and for CA II isoenzyme, 7%, 1798.56 EU/mg protein, and 42.38 respectively. Activity of CA was determined by measuring “CO2-hydratase activity”. Purity control was checked by SDS-PAGE. In vitro inhibitory effect of Cu2+, Ag+, Cd2+, Ni2+ metal ions, and arsenic (V) oxide were also examined for both isozymes activities. Whereas Cu2+, Ag+, Cd2+, and Ni2+ ions showed inhibitory effects on both isozymes, arsenic (V) oxide showed activation effect. IC50 values were calculated by drawing activity %-[I] graphs for metal ions exhibiting inhibitory effects. IC50 values were determined as 3.39, 6.38, 13.52, and 206 μM for CA I isozyme and 6.16, 20.29, 46, and 223 μM for CA II isozyme respectively.

Keywords

Carbonic anhydrase Heavy metal Inhibition Purification 

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Copyright information

© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  • Müslüm Kuzu
    • 1
  • Veysel Çomaklı
    • 2
  • Ebru Akkemik
    • 3
  • Mehmet Çiftci
    • 4
  • Ömer İrfan Küfrevioğlu
    • 5
  1. 1.Faculty of PharmacyUniversity of Ağrı İbrahim ÇeçenAğrıTurkey
  2. 2.School of HealthyUniversity of Ağrı İbrahim ÇeçenAğrıTurkey
  3. 3.Faculty of Engineering and ArchitectureSiirt UniversitySiirtTurkey
  4. 4.Faculty of Science and LettersBingöl UniversityBingölTurkey
  5. 5.Faculty of ScienceAtatürk UniversityErzurumTurkey

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