Heavy metal ion inhibition studies of human, sheep and fish alpha-carbonic anhydrases

DEMIRDAG R., YERLIKAYA E., SENTURK M., KÜFREVİOĞLU Ö. İ., SUPURAN C. T.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.28, sa.2, ss.278-282, 2013 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 28 Sayı: 2
  • Basım Tarihi: 2013
  • Doi Numarası: 10.3109/14756366.2011.640633
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.278-282
  • Anahtar Kelimeler: Carbonic anhydrase, metal ion, erythrocyte, sheep kidney, teleost fish, IN-VITRO, THERAPEUTIC APPLICATIONS, GLUTATHIONE-REDUCTASE, ISOZYMES I, ENZYME, PURIFICATION, ACTIVATORS
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrases (CAs, EC 4.2.1.1) were purified from sheep kidney (sCA IV), from the liver of the teleost fish Dicentrarchus labrax (dCA) and from human erythrocytes (hCA I and hCA II). The purification procedure consisted of a single step affinity chromatography on Sepharose 4B-tyrosine-sulfanilamide. The kinetic parameters of these enzymes were determined for their esterase activity with 4-nitrophenyl acetate as substrate. The following metal ions, Pb2+, Co2+, Hg2+, Cd2+, Zn2+, Se2+, Cu2+, Al3+ and Mn3+ showed inhibitory effects on these enzymes. The tested metal ions inhibited these CAs competitively in the low milimolar/submillimolar range. The susceptibility to various cations inhibitors differs significantly between these vertebrate alpha-CAs and is probably due to their binding to His64 or the histidine cluster.