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

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 "CO-hydratase activity". Purity control was checked by SDS-PAGE. In vitro inhibitory effect of Cu, Ag, Cd, Ni metal ions, and arsenic (V) oxide were also examined for both isozymes activities. Whereas Cu, Ag, Cd, and Ni ions showed inhibitory effects on both isozymes, arsenic (V) oxide showed activation effect. IC values were calculated by drawing activity %-[I] graphs for metal ions exhibiting inhibitory effects. IC 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.