Catecholamines, Monoamine Oxidase and Cholinesterase Activity in the Human Sympathetic Ganglion

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Abstract
Cholinesterase (ChE) and monoaniine oxidase (MAO) activities were measured in 17 surgically removed human lumbar sympathetic ganglia. Four further ganglia were obtained from accidentally killed men, autopsied at the Department of Forensic Medicine. ChEs were determined by automatic titration using acetylcholine, propionylcholine and butyrylcholine as substrates and specific ChE inhibitors (iso‐OMPA and 284C51). Of the total ChE activity (61.4 × 10‐‐3μmol/mg protein/min) 85%was found to be due to acetylcholinesterase (AChE, 53.6 × 10‐‐3μmol/mg protein/min) when acetylcholine was used as substrate. Propionylcholine (38.1 × 10‐‐3μmol/mg protein/min) was also mainly hydrolyzed by AChE (75%) and butyrylcholine (14.5 × 10‐‐3μmol/mg protein/min) by non‐specific cholinesterase (ns. ChE, 71 %). Histochemically, all the nerve cells showed AChE activity, most of them being moderately positive. Ns. ChE was chiefly present in the satellite cells and only a few weakly reactive nerve cells could be seen. MAO activity was measured fluorometrically with kynur‐amine as substrate (0.57 × 10‐‐3μmol/mg protein/min). Histochemically, all the nerve cells showed strong activity. Catecholamine fluorescence was weak in most of the ganglion cells. There were no significant differences in ChE or MAO activity between the different disease groups.