ISOLATION OF HYDROPHOBIC PROTEINS BINDING AMINO ACIDS: γ‐AMINOBUTYRIC ACID BINDING IN THE RAT CEREBRAL CORTEX

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<jats:title>Abstract</jats:title><jats:p>—The binding of [<jats:sup>14</jats:sup>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 [<jats:sup>14</jats:sup>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 [<jats:sup>14</jats:sup>C]GABA/μg of protein, with an apparent <jats:italic>K</jats:italic><jats:sub>d</jats:sub>= 30 μ<jats:sc>m</jats:sc>. The binding is competitively inhibited by bicuculline with a <jats:italic>K</jats:italic><jats:sub>i</jats:sub>= 273 μ<jats:sc>m</jats:sc>. These results are compared with those previously obtained on a GABA binding protein from crustacean muscle.</jats:p>

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