Glycerylphosphorylcholine diesterase activity of nervous tissue

Abstract

The hydrolysis of [alpha]-glycerylphosphorylcholine (GPC) by preparations of nervous tissue from various species was studied. GPC is rapidly hydrolyzed to [alpha]-glycerophosphate and choline by a diesterase present in these tissues. Although active at pH 7.4, maximal splitting of GPC was observed at pH 9.5. The addition of m[image] ethylene-diaminetetraacetic acid caused complete inhibition of activity, which could be largely restored by the addition of Mn2+, Mg2+, or Ca2+ ions. The diesterase is not inhibited by fluoride, cysteine, eserine, diisopropyl phosphorofluoridate or tri-o-cresyl phosphate.