Immobilized GABAA receptors and their ligand binding characteristics.

Article date: 1989/8/30

PubMed ID: 2550001

Journal name: Biochemical and biophysical research communications (ISSN: 0006-291X)


ConA-sepharose and polylysine-agarose beads effectively bound detergent-solubilized GABAA receptors from rat cerebrocortical membranes. The immobilized receptors showed a single class of high affinity binding sites specific for flunitrazepam or muscimol and displayed GABA-stimulated flunitrazepam binding. Maximal binding capacities of the ConA-immobilized receptor for the ligands were about three times greater than those of the polylysine-immobilized receptors. The relative affinities for each of the ligands were not affected by the method of receptor immobilization. The dissociation constants for muscimol of these immobilized receptors were somewhat dependent on the solubilizing agents used, but were considerably lower than those measured using extensively dialyzed rat cerebrocortical membranes.

This document is available from: http://directlinks.cc/files/muscimol/2550001.pdf

Author List: Im W B, Tai M M, Blakeman D P, Davis J P

Publication Types: Journal Article

Substances mentioned in the article: Ligands; Receptors, GABA-A; Concanavalin A; Polylysine; Muscimol; gamma-Aminobutyric Acid; Flunitrazepam;

Mesh terms: Animals; Cerebral Cortex/metabolism; Concanavalin A/metabolism; Flunitrazepam/metabolism; In Vitro Techniques; Ligands; Muscimol/metabolism; Polylysine/metabolism; Rats; Receptors, GABA-A/metabolism; Solubility; gamma-Aminobutyric Acid/metabolism;

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