A comparison of the effects of ionic strength on three preparations of acetylcholinesterase in the presence and absence of gallamine
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Cellular and Molecular Neuroscience
Reference14 articles.
1. Principles of Enzyme Kinetics;Cornish-Bowden,1976
2. The kinetics of human erythrocyte acetylcholine hydrolase before and after solubilization with Triton X-100;Cramb;Biochem. Soc. Trans.,1976
3. The influence of ionic strength on the interaction of quaternary drugs with mammalian acetylcholinesterase in relation to possible regulatory effects;Crone;J. Neurochem.,1973
4. Can allosteric effectors of acetylcholinesterase control the rate of ageing of the phosphonylated enzyme?;Crone;Biochem. Pharmac.,1974
5. Heterogeneity in the binding of acetylcholinesterase to Concanavalin A-agarose, and the isolation of a glycoprotein fraction;Crone,1979
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1. Hydrolysis in Pharmaceutical Formulations;Pharmaceutical Development and Technology;2002-01
2. Rate constants of carbamylation and decarbamylation of acetylcholinesterase for physostigmine and carbaryl in the presence of an oxime;Neurochemistry International;1994-02
3. Assessment of the competition between tacrine and gallamine for binding sites on acetylcholinesterase;Neurochemistry International;1991
4. Tacrine slows the rate of ageing of sarin-inhibited acetylcholinesterase;Neuroscience Letters;1989-05
5. Modification of the kinetic properties of Triton-solubilized rabbit brain acetylcholinesterase by allosteric effectors at low ionic strength;Neurochemistry International;1989
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