The effects of Ni2+, Co2+, and Mn2+ on human serum butyrylcholinesterase


Cokugras A., Cengiz D., Tezcan E.

JOURNAL OF PROTEIN CHEMISTRY, vol.22, no.6, pp.585-589, 2003 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 22 Issue: 6
  • Publication Date: 2003
  • Doi Number: 10.1023/b:jopc.0000005508.22140.28
  • Title of Journal : JOURNAL OF PROTEIN CHEMISTRY
  • Page Numbers: pp.585-589

Abstract

The effects of Ni2+, Co2+, and Mn2+ on human serum butyrylcholinesterase (BChE, acylcholine acylhydrolase E.C. 3.1.1.8) were investigated in this study. Inhibition kinetics of BChE were studied using butyrylthiocholine (BTCh) as substrate. The "1/v" versus "1/[BTCh]" plots in the absence (control plot) and in the presence of the metal ions intersected above 1/[BTCh]-axis for all trace elements. In addition, when the concentrations of the cations were increased at 4 mM BTCh, velocities decreased and drove to zero at high concentrations of the trace elements. These results demonstrate that Ni2+, Co2+, and Mn2+ are linear mixed-type inhibitors of BChE. alphaK(i) values have been determined as 53.20 mM, 152.25 mM, and 190.24 mM for Ni2+, Mn2+, and Co2+, respectively, by using nonlinear regression analysis. From the comparison of alphaK(i) values of the trace elements, it can be said that BChE has more affinty to binding Ni2+ than Co2+ and Mn2+.