Turkish Journal of Veterinary & Animal Sciences
DOI
-
Abstract
Carbonic anhydrase (CA) (carbonate hydrolyase: E. C. 4.2.1.1) from bovine lung was purified by a new method and characterized. The purification level was 4306-fold. The optimum temperature for maximum enzyme activity was 37.5°C. The optimum pH was 7.4, varying between 3.5 and 10.0. SDS-polyacryamide gel electrophoresis (3-10% discontinuous SDS-PAGE) showed two distinct bands for CA-IV. The molecular weights of the enzymes were found to be approximately 54.000 and 29.000, respectively. V_{max} and K_{M} values were calculated with p-nitrophenyl acetate as substrate (166.7 µmol/L*min, 5.59*10_{-2} M, respectively). Changes in enzyme activity were determined in the presence of some chemicals: sulfanilamide, NaN_3, KSCN, glucose, nicotine, nicotinamide, caffeine, CuSO_4 and MnCl_2; and some drinks: brandy, vodka, raki, whisky, cognac, beer, martini, apple liqueur, red wine, Pepsi, Yedigün, 7UP, Vimto and Coca-Cola (carbonated and non-carbonated).
Keywords
Carbonic anhydrase (IV), Alcohol, Nicotine, Nicotinamide, Caffeine
First Page
227
Last Page
233
Recommended Citation
DEMİR, NAZAN; NADAROĞLU, HAYRUNNİSA; and DEMİR, YAŞAR (2002) "Membrane Specific Carbonic Anhydrase (CA-IV) Expression in Bovine Lung: The Effects of Alcoholic and Non-Alcoholic Drinks," Turkish Journal of Veterinary & Animal Sciences: Vol. 26: No. 2, Article 5. Available at: https://journals.tubitak.gov.tr/veterinary/vol26/iss2/5
