@article {KRISHNAN621, author = {K. S. KRISHNAN and P. BALARAM}, title = {Nuclear Magnetic Resonance Studies of the Enzymatic Hydrolysis of Acetylcholine: a Critical Comment}, volume = {13}, number = {4}, pages = {621--624}, year = {1977}, publisher = {American Society for Pharmacology and Experimental Therapeutics}, 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.}, issn = {0026-895X}, URL = {https://molpharm.aspetjournals.org/content/13/4/621}, eprint = {https://molpharm.aspetjournals.org/content/13/4/621.full.pdf}, journal = {Molecular Pharmacology} }