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ISOLATION OF HYDROPHOBIC PROTEINS BINDING AMINO ACIDS: γ‐AMINOBUTYRIC ACID BINDING IN THE RAT CEREBRAL CORTEX
Author(s) -
Fiszer de Plazas Sara,
Robertis E. De
Publication year - 1975
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.1471-4159.1975.tb04366.x
Subject(s) - bicuculline , cerebral cortex , chemistry , binding protein , membrane , binding site , biochemistry , amino acid , biophysics , biology , gabaa receptor , endocrinology , receptor , gene
—The binding of [ 14 C]GABA to nerve‐ending membranes isolated from rat cerebral cortex follows a hyperbolic curve saturating at 0·4pmol/μg protein. This binding is about 60% inhibited by chloropromazine, and about 40%, inhibited by bicuculline. A hydrophobic protein fraction binding [ 14 C]GABA was separated from the total. lipid extract of nerve‐ending membranes. The binding follows a hyperbolic curve that saturates at 10·5 pmol of [ 14 C]GABA/μg of protein, with an apparent K d = 30 μ m . The binding is competitively inhibited by bicuculline with a K i = 273 μ m . These results are compared with those previously obtained on a GABA binding protein from crustacean muscle.