Characterization and inhibition effects of some metal ions on carbonic anhydrase enzyme from Kangal Akkaraman sheep

KOÇYİĞİT Ü. M., Taslimi P., GÜLÇİN İ.

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.32, sa.8, 2018 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 8
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1002/jbt.22172
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: carbonic anhydrase, characterization, enzyme purification, Kangal Akkaraman sheep, IN-VITRO INHIBITION, ISOENZYMES I, ESTERASE-ACTIVITIES, MANNICH-BASES, HCA I, ACETYLCHOLINESTERASE, DERIVATIVES, BUTYRYLCHOLINESTERASE, BROMOPHENOLS, PROFILES
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

In this work, the carbonic anhydrase (CA) enzyme was purified from Kangal Akkaraman sheep in Sivas, Turkey with specific activity value of 6681.57 EU/mg and yield of 14.90% with using affinity column chromatography. For designating the subunit molecular mass and enzyme purity. sodium dodecyl sulfate polyacrylamide gel electrophoresis method was used and single band for this procedure was obtained. The molecular mass of CA enzyme was found as 28.89 kDa. In this study, the optimum temperature and optimum pH were obtained from 30 and 7.5. V-max and K(m )values for p-nitrophenylacetate substrate of the CA were determined from Lineweaver-Burk graphs. Additionally, the inhibitory results of diverse heavy metal ions (He+, Fe2+, pb(2+), co(2+), A(g+), and Cu2+) on sheep were studied. Indeed, CA enzyme activities of Kangal sheep were investigated with using esterase procedure under in vitro conditions. The heavy metal concentrations inhibiting 50% of enzyme activity (IC50) and K-i values were obtained.