Tacrine protection of acetylcholinesterase from inactivation by diisopropylfluorophosphate: a circular dichroism study.

@article{Wu1989TacrinePO,
  title={Tacrine protection of acetylcholinesterase from inactivation by diisopropylfluorophosphate: a circular dichroism study.},
  author={Ching Shu Wu and Jen Tsi Yang},
  journal={Molecular pharmacology},
  year={1989},
  volume={35 1},
  pages={85-92}
}
Tacrine (1,2,3,4-tetrahydro-9-aminoacridine) showed an apparent noncompetitive inhibition of Torpedo acetylcholinesterase (AChE) with a dissociation constant, Ki, of 8.5 nM. It altered the CD bands of AChE in the near-UV region, which monitor the local conformation of aromatic side groups, but not those in the far-UV region, which measure the secondary structure. An extrinsic CD band was induced at 348 nm, with a molar ellipticity of 35,000 deg cm2 dmol-1 (bases on tacrine), when each AChE… CONTINUE READING