Binding constants for tetramethylammonium ion determined with irreversible inhibitors of acetylcholinesterase

Can J Biochem. 1976 Oct;54(10):918-20. doi: 10.1139/o76-130.

Abstract

The reversible binding constant (Ki) for tetramethylammonium ion (TMA) was determined from the decrease in the bimolecular rate constant (ki) observed with each of 21 organophosphate or carbamate inhibitors of acetylcholinesterase (EC 3.1.1.7). The Ki values obtained were reasonably constant (5.8 X 10(-4) +/- 0.38 M), and this is consistent with reports indicating that TMA binds to a single site on the enzyme.

MeSH terms

  • Carbamates
  • Cholinesterase Inhibitors*
  • Insecticides / pharmacology
  • Kinetics
  • Organophosphorus Compounds
  • Protein Binding
  • Quaternary Ammonium Compounds / pharmacology*
  • Structure-Activity Relationship

Substances

  • Carbamates
  • Cholinesterase Inhibitors
  • Insecticides
  • Organophosphorus Compounds
  • Quaternary Ammonium Compounds