Cholinesterase inhibition studies by stopped-flow instrumentation and automated data processing
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference18 articles.
1. Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues
2. Determination of the Bimolecular Rate Constant for the Reaction Between Organophosphorous Inhibitors and Esterases in the Presence of Substrate
3. Esters of Methanesulfonic Acid as Irreversible Inhibitors of Acetylcholinesterase
4. Affinity and Phosphorylation Constants for the Inhibition of Esterases by Organophosphates
5. Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate
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3. Enzymatic determination of N-methylcarbamate pesticides at the nanomolar level by the stopped-flow technique;Talanta;1991-11
4. Phosphylation kinetic constants and oxime‐induced reactivation in acetylcholinesterase from fetal bovine serum, bovine caudate nucleus, and electric eel;Journal of Toxicology and Environmental Health;1991-09
5. A generalized theoretical treatment of the kinetics of an enzyme-catalysed reaction in the presence of an unstable irreversible modifier;Journal of Theoretical Biology;1990-08
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