Sections of cat ciliary ganglia were stained for acetylcholinesterase activity by several modifications of the acetylthiocholine method in order to achieve optimal accuracy of cytological localization of the enzyme. These were compared by ordinary light and phase contrast microscopy with similar sections stained by standard techniques for Nissl substance, the Golgi apparatus, and the neurofibrillae, and by intravital methylene blue. The pattern of cytoplasmic distribution of acetylcholinesterase corresponded most closely with that of the Nissl substance. Following total inactivation of the ganglionic acetylcholinesterase by intravenously administered di-isopropyl fluorophosphate, the reappearance of the enzyme in vivo occurred at the same cytoplasmic sites prior to its reappearance at the cell membrane or preganglionic axonal terminations. These observations, and reports cited from the literature, provide support for the hypothesis that acetylcholinesterase is synthesized within the endoplasmic reticulum, then transported via its canaliculi to the surface of the cell and its processes, where its functional sites are oriented externally to the lipoidal membrane.

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