Specific lysis of noradrenergic synaptosomes by an antiserum to dopamine-beta-hydroxylase

An antiserum to dopamine-beta-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 mequiv./lK+ and exposed to a sub-maximal dose of antiserum, plus complement.