Turkish Journal of Chemistry
DOI
-
Abstract
In this study, carbonic anhydrase (CA: carbonate hydrolyase; E.C.4.2.1.1) was purified from adult {\it Nicotiana tabacum} leaves and studied biochemically. The enzyme was purified twice times by using (NH$_4)_2SO_4 precipation and DEAE-cellulose column chromatography, and its activity was determined for two different substrates (CO_2 and p-nitrophenyl acetate). The enzyme obtained from the ion exchange column was purified 40.7 fold and the purity was controlled by 3\%-10\% discontinuous SDS-PAGE. The pH of the purified enzyme varied between 6.0 and 7.2, the optimum being 6.9. V_{max} and K_m values were calculated with p-nitrophenyl acetate (0.1524 mM, 0.5446 mM, respectively) as substrate. The optimum temperature for the enzyme was 40^{\circ}C. The molecular weight of the enzyme and of the subunits were found to be approximately \approx137.000 daltons and \approx 22.800 daltons, respectively. The results indicate that 6 subunits are present. Changes in enzyme activity were determined in the presence of caffeine, nicotine, metal ions and some chemicals.
Keywords
Carbonic anhydrase, {\it Nicotiana tabacum, } caffeine, nicotine
First Page
111
Last Page
117
Recommended Citation
DEMİR, Nazan and DEMİR, Yaşar (1997) "Carbonic Anhydrase From Nicotiana Tabacum Leaves," Turkish Journal of Chemistry: Vol. 21: No. 2, Article 7. Available at: https://journals.tubitak.gov.tr/chem/vol21/iss2/7
