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Neurochemical Characterization of an Antimony‐Choline Analog in Rat Cortical Synaptosomes
Author(s) -
Meyer Edwin M.,
Barrnett Russell J.,
Cooper Jack R.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb03950.x
Subject(s) - choline , cholinergic , chemistry , neurochemical , acetylcholine , synaptosome , biochemistry , acetylation , biophysics , neuroscience , endocrinology , biology , in vitro , gene
An analog of choline, in which nitrogen was replaced by antimony, was neurochemically characterized in rat cortical synaptosomes. It was found to be a substrate for several cholinergic enzymes, transported by a Na + ‐dependent, hemicholinium‐3‐sensitive process, acetylated, and subsequently released by depolarization in a calcium‐dependent manner. Sb‐choline also competed with choline for Na + ‐dependent uptake and for acetylation by [ 14 C]acetyl‐CoA in synaptosomes. These results suggest that Sb‐choline and its acetylated product should be useful substrates for the x‐ray microanalytical localization of cholinergic pools in intact nerve terminals.