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Neurochemical Characterization of an Antimony‐Choline Analog in Rat Cortical Synaptosomes

Abstract: 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 [14C]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.