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

• Published in: Journal of Protein Chemistry Vol. 22; no. 6; pp. 585 - 589
• Main Authors: Cokuğraş, A Neşe, Cengiz, Doğan, Tezcan, E Ferhan
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01-08-2003
• Subjects: Butyrylcholinesterase - blood; Carbon dioxide; Cations; Cholinesterase Inhibitors - pharmacology; Cobalt; Cobalt - pharmacology; Enzyme kinetics; Humans; Kinetics; Manganese - pharmacology; Metal ions; Molecular biology; Nickel - pharmacology; Proteins; Regression analysis; Substrates; Trace elements
• ISSN: 0277-8033; 1572-3887; 1573-4943
• DOI: 10.1023/b:jopc.0000005508.22140.28

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+.