Diazepam enhancement of low affinity GABA binding to rat brain membranes

Diazepam (3 nM–3 μM) enhanced GABA binding to well-washed synaptosomal membranes in a concentration-dependent manner. Half maximal enhancement occurred at 20 nM diazepam. Kinetic analysis by non-linear Scatchard analysis revealed that the primary action of diazepam was to increase the affinity of GA...

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Veröffentlicht in:Neuroscience letters 1982-03, Vol.29 (1), p.63-66
Hauptverfasser: Skerritt, John H., Willow, Max, Johnston, Graham A.R.
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container_title Neuroscience letters
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creator Skerritt, John H.
Willow, Max
Johnston, Graham A.R.
description Diazepam (3 nM–3 μM) enhanced GABA binding to well-washed synaptosomal membranes in a concentration-dependent manner. Half maximal enhancement occurred at 20 nM diazepam. Kinetic analysis by non-linear Scatchard analysis revealed that the primary action of diazepam was to increase the affinity of GABA binding to a low affinity site. These results support electrophysiological and other biochemical observations of benzodiazepine-GABA interactions.
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subjects Animals
Binding Sites - drug effects
Brain - anatomy & histology
Brain - metabolism
Cell Membrane - metabolism
Diazepam - pharmacology
gamma-Aminobutyric Acid - metabolism
Kinetics
Rats
Synaptosomes - metabolism
Synaptosomes - ultrastructure
title Diazepam enhancement of low affinity GABA binding to rat brain membranes
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