Kinetic characterization of all steps of the interaction between acetylcholinesterase and eserine

This publication has 16 references indexed in Scilit:

• Physostigmine analogs anticholinesterases: effects of the lengthening of the N-carbamic chain of the inhibition kinetics
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
• On the inhibition of cholinesterase by d-tubocurarine
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
• A nonlinear least squares program based on differential equations, MULTI (RUNGE), for microcomputers.
  Journal of Pharmacobio-Dynamics, 1983
• Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands
  Biochemistry, 1980
• Tight-binding inhibitors—I
  Biochemical Pharmacology, 1975
• Cholinesterase Inhibitors: Structure of Eserine
  Nature, 1973
• Inhibition of cholinesterase by carbamates. A new kinetic approach
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
• Carbamylation and Binding Constants for the Inhibition of Acetylcholinesterase by Physostigmine (Eserine)
  Science, 1966
• A new and rapid colorimetric determination of acetylcholinesterase activity
  Biochemical Pharmacology, 1961
• Inhibition of Esterases by the Fluorides of Organic Acids
  Nature, 1954