Michael Newton

TL;DR: The complete amino-acid sequence of an acetylcholinesterase inferred from the sequence of a complementary DNA clone is reported and the 575-residue protein shows significant homology with the C-terminal portion of thyroglobulin8.

TL;DR: Northern blot and RNAase protection analyses indicate that the cDNA clones were derived from the acetylcholinesterase transcript that predominates in most expressing tissues, in contrast, erythroid cells are enriched in an mRNA species whose sequence diverges from that of the c DNA in the region encoding the C-terminus of the enzyme.

TL;DR: Differences in specificity between species, and among cholinergic synapses within an organism, may provide a means for selectivity in effects caused by administration of a false precursor.

TL;DR: Recent studies which suggest the molecular structure of acetylcholinesterase resembles a secreted rather than an integral membrane protein are reviewed.

TL;DR: The use of false transmitters as pharmacological probes has provided evidence for different structural specificities at each of the steps involved in acetylcholine turnover as mentioned in this paper, which may provide a means for selectivity in effects caused by administration of a false precursor.