Purification and characterization of acetylcholinesterase from sheep liver and inhibition by some painkillers

GULOGLU O., Turkoglu V., CELIK ı.

ASIAN JOURNAL OF CHEMISTRY, vol.18, no.2, pp.1097-1103, 2006 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 18 Issue: 2
  • Publication Date: 2006
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1097-1103
  • Van Yüzüncü Yıl University Affiliated: Yes


In this study, acetylcholinesterase (AChE; EC was purified from sheep liver by affinity chromatography. The purification rate was found 3541.7 fold. The purification control of enzyme was done with sodium dodesilsulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH, ionic strength and temperature of enzyme were determined. The optimal pH and the optimum temperature were 7.5-8.5 and 35 degrees C respectively. The highest activity was seen in concentration of 0.2 M (NH4)(2)SO4 as ionic strength. On the other hand, the inhibition effects of some painkiller, (paracetamol + caffein), (neostigmin methylsulfate) and (paracetamol + propifenazon + caffein) were investigated in this study. According to results, the I-50 values are 1.27 X 10(-3), 1.02 x 10(-4) and 1.236 M respectively. Also, K-i values are determined as 1.246 x 10(-3), 4.326 x 10(-5) and 1.646 x 10(-3) mol(-1) min(-1) respectively.