Open AccessAdenosine Triphosphatase Activity Associated with Purified Cholinergic Synaptic Vesicles of Torpedo marmorata
Author(s) -
BREER Heinz,
MORRIS Stephen J.,
WHITTAKER Victor P.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11884.x
Subject(s) - vesicle , torpedo , synaptic vesicle , acetylcholine , atpase , glycine , acetylcholinesterase , chemistry , biochemistry , cholinergic , biophysics , biology , enzyme , chromatography , membrane , endocrinology , amino acid , acetylcholine receptor , receptor
A rapid method for purifying Torpedo electric organ vesicles is described, which employs an iso‐osmotic continuous sucrose‐glycine gradient followed by chromatography on CPG‐10‐3000 porous glass beads. The synaptic vesicles have a buoyant density of 1.057 g/ml. The purified vesicles are free of cholinesterase, lactate dehydrogenase and Na + ,K + ‐stimulated ATPase activity. They contain a ouabaininsensitive, Na + ,K + ‐inhibited, Mg 2+ ,Ca 2+ ‐stimulated ATPase activity. This is further stimulated by acetylcholine but not by choline.