Identification of butyrylcholinesterase adducts after inhibition with isomalathion using mass spectrometry: difference in mechanism between (1R)- and (1S)-stereoisomers.

@article{Doorn2001IdentificationOB,
  title={Identification of butyrylcholinesterase adducts after inhibition with isomalathion using mass spectrometry: difference in mechanism between (1R)- and (1S)-stereoisomers.},
  author={Jonathan A. Doorn and Michael Schall and Douglas A. Gage and Todd T. Talley and Charles M. Thompson and Rudy J. Richardson},
  journal={Toxicology and applied pharmacology},
  year={2001},
  volume={176 2},
  pages={73-80}
}
Previous kinetic studies found that butyrylcholinesterase (BChE) inhibited by (1R)-isomalathions readily reactivated, while enzyme inactivated by (1S)-isomers did not. This study tested the hypothesis that (1R)- and (1S)-isomers inhibit BChE by different mechanisms, yielding distinct adducts identifiable by peptide mass mapping with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Equine BChE (EBChE) was inhibited to <10% of control activity with each… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 10 extracted citations

Similar Papers

Loading similar papers…