Acetylcholinesterase and Acetylcholine Receptor

This research seeks information about the properties and amino acid content of the active site of acetylcholinesterase AcChE. It is based largely on the view that the subsite at which the positively charged Beta-substituent of the natural substrate, acetylcholine AcCh, binds is not anionic, as is generally accepted, but uncharged and complementary to the trimethyl substituted character of that substituent. The subsite would be more specifically explored by uncharged reagents, while positive reagents would react at peripheral negative sites. Thus, uncharged irreversible and reversible inhibitors and substrates are obtained or synthesized and their reactions with the enzyme are studied. Keywords Torpedo nobiliana Chromatography Electrophoresis.