Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations.
Open Access
- 30 November 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (34) , 20735-20738
- https://doi.org/10.1016/s0021-9258(17)45277-x
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Structure of the gene for human butyrylcholinesterase. Evidence for a single copyBiochemistry, 1990
- Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesChemical Reviews, 1987
- Sequence determination of a peptide fragment from electric eel acetylcholinesterase, involved in the binding of quaternary ammoniumFEBS Letters, 1986
- Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequenceNature, 1986
- Polymorphism of Acetylcholinesterase in Discrete Regions of the Developing Human Fetal BrainJournal of Neurochemistry, 1985
- Different forms of insensitive acetylcholinesterase in insecticide-resistant house flies (Musca domestica)Pesticide Biochemistry and Physiology, 1984
- Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligandsBiochemistry, 1980
- Hydrolysis of suxamethonium by different types of plasmaBritish Journal of Pharmacology, 1969
- Complete Pseudocholinesterase Deficiency: Genetic and Immunologic Characterization*Journal of Clinical Investigation, 1965
- Differential inhibition of the serum cholinesterase phenotypes by solanine and solanidineAnnals of Human Genetics, 1962