Abstract
The localization of acetylcholinesterase activity in the fine structure of mouse and human neuromuscular junctions was studied by the method of Barrnett and Palade. A formolsucrose solution was used for primary fixation followed by osmification. It was found that deposits of lead sulphide, the product of the histochemical reaction, were found in axonal and sarcoplasmic mitochondria and most prominently in the primary and secondary synaptic clefts of the subneural apparatus. Rarely were reactive sites found near the M-band. Control experiments utilizing inhibitors and high concentrations of Pb(NO3)2 were performed. The possible significance of acetylcholinesterase activity in the areas described is discussed.