Molecular interactions of acetylcholinesterase with senile plaques

Inestrosa, N. C.; Alarcon, R

Keywords: substrate, inhibition, enzyme, amyloid, animals, complex, protein, cell, gene, inactivation, disease, alpha, beta, mutation, humans, human, paper, interaction, acetylcholinesterase, assembly, formation, drug, molecular, alzheimer, plaque, activity, neuropathology, helix, plaques, effect, conference, senile

Abstract

Acetylcholinesterase (ACHE) present in Alzheimer plaques is resistant to low pH, anti-ChE inhibitors and high substrate concentrations in comparison with the free enzyme. Kinetic and pharmacological studies of AChE-amyloid complexes indicate that steric hindrance by the amyloid over the gorge and the peripheral site of AChE is responsible for these effects.

Más información

Título de la Revista: JOURNAL OF PHYSIOLOGY-PARIS
Volumen: 92
Número: 5-6
Editorial: EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Fecha de publicación: 1998
Página de inicio: 341
Página final: 344
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-0032440687&partnerID=q2rCbXpz
DOI:

10.1016/S0928-4257(99)80002-3

Notas: ISI