Abstract
A histochemical procedure has been developed for the demonstration of choline acetyltransferase activity. This procedure is based upon the formation of an insoluble lead mercaptide from coenzyme A (CoASH), a product of the enzymatic reaction. Optimal conditions for the precipitation of the lead mercaptide are defined. The localization of the reaction product in the rat spinal cord is restricted to the neuronal element. Heavy deposition of reaction product in the perikaryon was noted for the anterior motor neurons; some of the other neurons were negative. Boutons terminaux were visible on the surface of all neurons studied. A combination of quantitative radiochemical data, enzyme solubilization, copper inhibition and the histologic distribution of the reaction product is discussed in relation to the specificity of the procedure for the differential localization of choline acetyltransferase and nonspecific acetyl-CoA hydrolase activities.
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