Abstract
Studies at 100 MHz of the hydrolysis of acetylcholine by brain membrane-bound acetylcholinesterase show that the N-methyl resonance acquires a doublet character as the hydrolysis proceeds. These results provide a simple explanation for the time-dependent NMR line broadening observed earlier for the interaction of acetylcholine with purified acetylcholinesterase.
ACKNOWLEDGMENT We thank the Department of Organic Chemistry, Indian Institute of Science, for use of the HA-100 spectrometer.
- Copyright © 1977 by Academic Press, Inc.
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