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Choline acetyltransferase was purified from rat striata by several sequential column chromatographic separations on Sepharose 4B, hydroxylapatite, Sephadex G-150 and CM-Sephadex, and finally by elution of enzymatically active protein from gel slices. Conventional rabbit and monoclonal antibodies to the enzyme were produced. Monoclonal antibodies were radiolabeled in vivo and used for specific immunoradioautographic localization of choline acetyltransferase in cholinergic neurons by light and electron microscopy.
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