The nature of the reaction of organophosphorus compounds and carbamates with esterases.
- 1 January 1971
- journal article
- Vol. 44, 25-30
Abstract
This paper outlines our knowledge of the reaction of organophosphorus compounds and carbamates with esterases, examples of particular aspects of the reaction being confined to cholinesterases, although the general principles discussed apply to all B-esterases. Mathematical expressions are given for the different rate constants, and some of the factors that may affect the response of insect and mammalian cholinesterases to organophosphorus compounds and carbamates are discussed.This publication has 32 references indexed in Scilit:
- Effect of tetraethylammonium ions on the affinity and phosphorylation or carbamylation constants of malaoxon, Tetram and Temik with acetylcholinesteraseBiochemical Pharmacology, 1970
- Detoxification of Diazinon by Subcellular Fractions of Diazinon-resistant and Susceptible HousefliesNature, 1969
- Affinity and phosphorylat1on constants of a series of O,O-dialkyl malaoxons and paraoxons with acetylcholinesteraseBiochemical Pharmacology, 1969
- The reaction of acetylcholinesterase with methanesulfonyl esters of quaternary quinolinium compoundsBiochemical Pharmacology, 1969
- The acute toxicity of dichloroalkyl aryl phosphates in relation to chemical structureBiochemical Pharmacology, 1967
- Di-(2-chloroethyl) aryl phosphatesBiochemical Pharmacology, 1964
- Chemical nature of the DFP-binding site of pseudocholinesteraseBiochimica et Biophysica Acta, 1959
- The turnover number of ali-esterase, pseudo- and true cholinesterase and the combination of these enzymes with diisopropylfluorophosphonateBiochimica et Biophysica Acta, 1954
- Effect of salt on the hydrolysis of acetylcholine by cholinesterasesArchives of Biochemistry and Biophysics, 1952
- Properties and behavior of purified human plasma cholinesterase. III. Competitive inhibition by prostigmine and other alkaloids with special reference to differences in kinetic behaviorArchives of Biochemistry and Biophysics, 1951