Abstract
Gamma-aminobutyric acid (GABA) binding sites were solubilized from rat brain synaptosomal fractions by extraction with a combination of sodium deoxycholate and potassium chloride. Specific 3H-GABA binding to the solubilized fraction was saturable with the apparent dissociation constant, Kd = 23.4 ± 0.2 nM. GABA agonists and an antagonist inhibited the binding. The relative potencies of these drugs in competing for 3H-GABA binding to the solubilized fraction are in good agreement with findings with the membrane fraction, suggesting that the binding sites in the solubilized fraction retain the characteristics of membrane-bound GABA receptor. The sedimentation coefficient value of 3H-GABA binding site was estimated to be 11.3S by sucrose density gradient centrifugation, and this value was identical with that of 3H-flunitrazepam binding site in the same solubilized fraction.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call