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G‐proteins in Torpedo marmorata electric organ Differential distribution in pre‐ and post‐synaptic membranes and synaptic vesicles
Author(s) -
Toutant Madeleine,
Bockaert Joël,
Homburger Vincent,
Rouot Bruno
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80190-4
Subject(s) - torpedo , synaptic vesicle , vesicle , protein subunit , neurotransmission , membrane , biology , microbiology and biotechnology , synaptosome , biochemistry , biophysics , chemistry , acetylcholine receptor , receptor , gene
The nature of the G‐proteins present in the pre‐ and post‐synaptic plasma membranes and in the synaptic vesicles of cholinergic nerve terminals purified from the Torpedo electric organ was investigated. In pre‐ and post‐synaptic plasma membranes, Bordetella pertussis toxin, known to catalyze the ADP‐ribosylation of the α‐subunit of several G‐proteins, labels two substrates at 41 and 39 kDa. The 39 kDa subunit detected by ADP‐ribosylation in the synaptic plasma membrane fractions was immunologically similar to the G o α‐subunit purified from calf brain. In contrast to bovine chromaffin cell granules, no G‐protein could be detected in Torpedo synaptic vesicles either by ADP‐ribosylation or by immunoblotting.