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

Kuzu M., Comakli V., Akkemik E., Ciftci M., KÜFREVİOĞLU Ö. İ.

FISH PHYSIOLOGY AND BIOCHEMISTRY, cilt.44, sa.4, ss.1119-1125, 2018 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 44 Sayı: 4
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1007/s10695-018-0499-8
  • Dergi Adı: FISH PHYSIOLOGY AND BIOCHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1119-1125
  • Anahtar Kelimeler: Carbonic anhydrase, Heavy metal, Inhibition, Purification, TROUT ONCORHYNCHUS-MYKISS, SALMO-TRUTTA LABRAX, RAINBOW-TROUT, ENZYME-ACTIVITY, KINETIC-PROPERTIES, PURIFICATION, LIVER, VITRO, IONS, CADMIUM
  • Atatürk Üniversitesi Adresli: Evet

Özet

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 mu M for CA I isozyme and 6.16, 20.29, 46, and 223 mu M for CA II isozyme respectively.