In vitro inhibitory effects of some heavy metals on human erythrocyte carbonic anhydrases

Ekinci D., BEYDEMİR Ş., KÜFREVİOĞLU Ö. İ.

Journal of Enzyme Inhibition and Medicinal Chemistry, cilt.22, sa.6, ss.745-750, 2007 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 22 Sayı: 6
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1080/14756360601176048
  • Dergi Adı: Journal of Enzyme Inhibition and Medicinal Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.745-750
  • Anahtar Kelimeler: Carbonic anhydrase, HCA-1, HCA-II, Heavy metals, Inhibition
  • Bilecik Şeyh Edebali Üniversitesi Adresli: Evet

Özet

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-1 and a yield of 30% and CA-II isozyme was purified with a specific activity of 8000-EUmg-1 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 1.45 mM for HCA-I and 0.059, 1.382 and 0.32 mM for 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.