Specific lysis of noradrenergic synaptosomes by an antiserum to dopamine‐β‐hydroxylase

An antiserum to dopamine‐β‐hydroxylase purified from bovine adrenal medulla, acting in the presence of complement, caused the release of 12% of lactate dehydrogenase, 20% of tyrosine hydroxylase activity, and 40% of noradrenaline (NA) content from synaptosomes prepared from rat brain cerebral cortex. Uptake of [³H]NA was reduced by 54%. Anti‐serum alone or complement alone were without action. The antiserum plus complement had no effect on choline uptake and did not release choline acetyltransferase, glutamate decarboxylase, dopamine or 5‐hydroxytryptamine. These results suggest selective lysis of noradrenergic terminals had occurred. An enhancement of lysis was not observed when synaptosomes were stimulated with 75 K⁺ and exposed to a sub‐maximal dose of antiserum, plus complement.