Acetylcholinesterase and Acetylcholine Receptor.
Annual rept. 15 Sep 84-14 Sep 85,
BRANDEIS UNIV WALTHAM MA DEPT OF CHEMISTRY
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We are studying the properties of the active site, and the region peripheral to it, of acetylcholinesterase AcChE, the enzyme which hydrolyzes and thus terminates the action of the important neurotransmitter acetylcholine AcCh. We have studied the response of the enzyme to synthesized substrates and inhibitors of varied structure for indications about the parts of the enzyme that are complementary to these substrates. From this information radioactive active-site-directed irreversible inhibitors have been designed for use in labeling amino acids in the active site. In this work AcChE was isolated from Torpedo nobiliana. Novel uncharged reversible inhibitors were also prepared for study of their action on the AcCh receptor by Professor J.B. Cohen, Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis.