The methamidophos-inactivated cholinesterase (ChE) was reactivated by dialysis, whereas, the acephate-inactivated ChE was not reactivated by dialysis. The acephate-inactivated ChE was also not reactivated by Pyridine-2-aldoxime methiodide (2-PAM). The kinetic properties of control-ChE were significantly different from the kinetic properties of the acephate-exposed- dialyzed ChE. However, the kinetic properties of control ChE were similar to the kinetic properties of the methamidophos-exposed-dialyzed ChE. It is proposed that acephate irreversibly binds to a peripheral 'allosteric' site in ChE and alters the kinetic properties of the ChE active sites.
|Original language||English (US)|
|Number of pages||2|
|Journal||Medical Science Research|
|State||Published - Jan 1 1988|