Differential inhibition of human erythrocyte acetylcholinesterase by polyphenols epigallocatechin-3-gallate and resveratrol. Relevance of the membrane-bound form.

@article{Salazar2017DifferentialIO,
  title={Differential inhibition of human erythrocyte acetylcholinesterase by polyphenols epigallocatechin-3-gallate and resveratrol. Relevance of the membrane-bound form.},
  author={Paula B Salazar and Alejandro de Athayde Moncorvo Collado and Ver{\'o}nica Canal-Mart{\'i}nez and Carlos Minahk},
  journal={BioFactors},
  year={2017},
  volume={43 1},
  pages={73-81}
}
The activity of acetylcholinesterase (AChE) from human erythrocytes was tested in the presence of the phenolic compounds resveratrol and epigallocatechin-3-gallate (EGCG). Even though the stilbene barely changed this enzymatic activity, EGCG did inhibit AChE. Importantly, it preferentially acted on the membrane-bound enzyme rather than on its soluble form. Actually, it was shown that this flavonoid may bind to the red blood cell membrane surface, which may improve the interaction between EGCG… CONTINUE READING
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