Abstract
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) |
|---|---|
| Pages (from-to) | 727-728 |
| Number of pages | 2 |
| Journal | Medical Science Research |
| Volume | 16 |
| Issue number | 14 |
| State | Published - Jan 1 1988 |