A cell-surface antigen of cholinergic nerve terminals recognized by antisera to choline acetyltransferase

Abstract

An antiserum to choline acetyltransferase, partially purified from bovine brain (anti-ChAT 1), when incubated with synaptosomes prepared from rat cerebral cortex in the presence of complement caused release of 10% of lactate dehydrogenase and 27% of ChAT. Sodium-dependent uptake of choline was totally abolished. Similar results were obtained when an antiserum to ChAT highly purified from pig brain (anti-ChAT 2) was used under similar conditions. These treatments had no effect on noradrenaline uptake and did not release glutamate decarboxylase. The results suggest selective lysis of cholinergic synaptosomes had occurred. A similar selective lysis was also observed when synaptosomes prepared from guinea pig cerebral cortex were used. Anti-ChAT 2 also inhibited choline uptake in a complement-independent manner.