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

作者：Sara Fiszer de Plazas, Eduardo D. P. De Robertis · 发表于：Journal of Neurochemistry · 年份：1975 · DOI：10.1111/j.1471-4159.1975.tb04366.x · 被引用次数：40 · 研究领域：Biochemical effects in animals、Neuroscience and Neuropharmacology Research、Lipid Membrane Structure and Behavior

Abstract —The binding of [14C]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 [14C]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 [14C]GABA/μg of protein, with an apparent Kd= 30 μm. The binding is competitively inhibited by bicuculline with a Ki= 273 μm. These results are compared with those previously obtained on a GABA binding protein from crustacean muscle.