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Inhibition of [ 3 H]GABA Binding to Postsynaptic Receptors in Human Cerebellar Synaptic Membranes by Carboxyl and Amino Derivatives of GABA
Author(s) -
Breckenridge Robin J.,
Nicholson Sydney H.,
Nicol Alan J.,
Suckling Colin J.,
Leigh Beatrice,
Iversen Leslie
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb04469.x
Subject(s) - postsynaptic potential , membrane , gabaa receptor , chemistry , synaptic membrane , synaptic cleft , receptor , amino acid , biophysics , stereochemistry , biochemistry , neurotransmission , biology
Fifty synthetic analogues of GABA were tested for their ability to interact with GABA receptors, using [ 3 H]GABA binding to human cerebellar membranes as an in vitro model. The most active compounds were found to be aliphatic and heterocyclic aminosulphonic acids. Compounds with highly substituted nitrogen atoms were only weakly active unless a long alkyl chain, which can interact with the postsynaptic membrane, was present. It was concluded that a pyramidal nitrogen atom is favoured for binding of GABA analogues to human cerebellar membranes