The effect of ethanol on erythrocyte carbonic anhydrase isoenzymes activity:: An in vitro and in vivo study

ÇOBAN T. A., Beydemir Ş., GÜLÇİN İ., Ekinci D.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.23, no.2, pp.266-270, 2008 (SCI-Expanded) identifier identifier identifier


The ethanol is a widely consumed as sedative-hypnotic drug throughout the world. In this study, the effects of ethanol were investigated on carbonic anhydrase (CA) enzyme activities both in vitro in human erythrocyte and in vivo in Sprague-Dawley rat erythrocyte. For in vitro study, the human carbonic anhydrase-I (HCA-I) and -II (HCA-II) are purified by Sepharose 4B-L-tyrosine-sulphanilamide affinity chromatography. In vivo CA enzyme activity was determined colorimetrically by using CO2-hydration method of Wilbur and Anderson. Rat blood samples were taken from each rat before and after the ethanol administration at different times (I h, 3 h, and 5 h). Rat erythrocyte CA activity was significantly inhibited by pharmacological dosage of the ethanol (2 for up to 3 h (p < 0.001) following intraperitoneally administration. The ethanol showed in vitro inhibitory effects on HCA-I and HCA-II hydratase activity, determined by colorimetrically using the CO2-hydratase method. The inhibitor concentrations causing up to 50% inhibition (IC50) were 2.09 M for HCA-I (r(2):0.9273) and 1.83 M for HCA-II (r(2):9749). In conclusion, it was demonstrated that carbonic anhydrase enzyme in erythrocytes was significantly inhibited by the ethanol both in in vitro and in vivo.