Catalysis by Acetylcholinesterase. Substrate-Mediated Perturbations.

Abstract

The characteristics of the inhibition of acetylcholinesterase by hexamethylenebis(dimethyl(3-phthalimidopropyl)ammonium bromide) (PTP) are both qualitatively and quantitatively different when examined in the presence of the substrates acetylcholine (ACh) and phenyl acetate (PA). Results are interpreted in terms of the Rosenberry and Bernhard (1972) model for acetylcholinesterase catalysis, which involves specific regulatory and inhibitory sites on the enzyme, and offer additional support for this model. Perturbation of the enzyme via such regulatory sites may provide new approaches to prophylaxis and therapy for poisoning by anticholinesterase compounds.

Document Details

Document Type
Technical Report
Publication Date
Oct 01, 1974
Accession Number
ADA001502

Entities

People

  • George M. Steinberg
  • Joseph W. Amshey Jr.

Tags

DTIC Thesaurus Topics

  • Acetylcholinesterases
  • Catalysis
  • Enzyme Inhibitors
  • Enzymes
  • Inhibition
  • Perturbations
  • Poisoning
  • Preventive Medicine
  • Substrates

Fields of Study

  • Biology

Readers

  • Neurotoxicology
  • Systems Analysis and Design