Kuzu, MuslumComakli, VeyselAkkemik, EbruCiftci, MehmetKufrevioglu, Omer Irfan2024-12-242024-12-2420180920-17421573-5168https://doi.org/10.1007/s10695-018-0499-8https://hdl.handle.net/20.500.12604/6052In 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.eninfo:eu-repo/semantics/closedAccessCarbonic anhydraseHeavy metalInhibitionPurificationArticle44411191125Q2WOS:000437000200010Q12-s2.0-850451093152962948910.1007/s10695-018-0499-8