Stopped-flow studies of the inhibition of acetylcholinesterase by organophosphates in the presence of substrate
- 1 June 1974
- journal article
- Published by Elsevier in Pesticide Biochemistry and Physiology
- Vol. 4 (2) , 239-244
- https://doi.org/10.1016/0048-3575(74)90103-5
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrateBiochemistry, 1973
- Structural properties of acetylcholinesterase from eel electric tissue and bovine erythrocyte membranesBiochemistry, 1973
- Transients and Relaxation Kinetics of Enzyme ReactionsAnnual Review of Biochemistry, 1971
- Kinetic Evidence of Multiple Reversible Cholinesterases Based on Inhibition by OrganophosphatesJournal of Biological Chemistry, 1969
- Affinity and Phosphorylation Constants for the Inhibition of Esterases by OrganophosphatesScience, 1964
- Determination of the Bimolecular Rate Constant for the Reaction Between Organophosphorous Inhibitors and Esterases in the Presence of SubstrateNature, 1963
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961
- Reaction of plasma albumin with i-naphthyl N-methylcarbamate and certain other estersBiochimica et Biophysica Acta, 1959
- Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analoguesBiochemical Journal, 1950
- CHROMOGENIC SUBSTRATESPublished by Elsevier ,1947