Abstract
THE enzyme acetylcholinesterase (AChE), which catalyses the hydrolysis of acetylcholine to choline and acetic acid, has been the subject of a great deal of interest not only in connexion with its structure and mode of action but also because of the role usually attributed to acetylcholine in the transmission of nerve stimuli1. We have carried out experiments to investigate the effect of heat on the activity and antigenic properties of this enzyme, and these have revealed that the activity of the enzyme can be restored after heat denaturation by adding antibodies to the native enzyme. What follows is a report on these experiments.
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References
Davies, D. R., and Green, A. L., Adv. Enzymol., 20, 283 (1958).
Ellman, G. L., Courtney, D. K., Andrews, V., jun., and Featherstone, R. M., Biochem. Pharmacol., 7, 88 (1961).
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MICHAELI, D., PINTO, J. & BENJAMINI, E. Restoration of Enzyme Activity of Heat-denatured Acetylcholinesterase by Antibodies to the Native Enzyme. Nature 213, 77–78 (1967). https://doi.org/10.1038/213077a0
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DOI: https://doi.org/10.1038/213077a0
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