Akademik Veri Yönetim Sistemi
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.22, sa.6, ss.745-750, 2007 (SCI-Expanded)
The inhibition of two human carbonic anhydrase (HCA, EC 4.2.1.1) isozymes, the cytosolic HCA I and II, with heavy metal salts of Pb( II), Co(II) and Hg( II) has been investigated. Human erythrocyte CA- I isozyme was purified with a specific activity of 920 EUmg 21 and a yield of 30% and CA- II isozyme was purified with a specific activity of 8000EUmg 21 and a yield of 40% using Sepharose-4B-L tyrosine-sulfanilamide affinity gel chromatography. The overall purification was approximately 104-fold for HCA-I and 900-fold for HCA-II. The inhibitory effects of different heavy metals ( lead, cobalt and mercury) on CA activity were determined at low concentrations using the esterase method under in vitro conditions. Ki values for these metals were calculated from Lineweaver-Burk graphs as 1.0, 3.22 and 1.45mMfor HCA-I and 0.059, 1.382 and 0.32mMfor HCA-II respectively. Lead was a noncompetitive inhibitor for HCA-I and competitive for HCA-II, cobalt was competitive for HCA-I and noncompetitive for HCA-II and mercury was uncompetitive for both HCA-I and HCA-II. Lead was the best inhibitor for both HCA-I and HCA-II.