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Photolabeling of brain membrane proteins by lysergic acid diethylamide

Anne C. Mahon, Paul R. Hartig

Life Sciences April 5, 1982 DOI: 10.1016/0024-3205(82)90660-9 (opens in new tab)

Study at a glance

AI-extracted from the abstract
Characteristics Laboratory experiment Peer reviewed
Population Bovine caudate membranes
Intervention ultraviolet light illumination
Topics LSD
Citations 7
Key findings Photolabeling of bovine caudate membranes with 3H-LSD is not specific for LSD binding sites associated with neurotransmitter receptors and can occur under room lighting, potentially introducing artifacts into receptor binding assays.

Abstract

3H-Lysergic acid diethylamide (3H-LSD) is irreversibly incorporated into bovine caudate membranes during ultraviolet light illumination. The incorporated radioligand apparently forms a covalent bond with a subpopulation of the membrane proteins. Although the photolabeling pattern differs significantly from the Coomassie blue staining pattern on SDS gels, the photolabeling is apparently not specific for LSD binding sites associated with neurotransmitter receptors. 3H-LSD photolabeling can occur during prolonged exposure of membrane samples to room lighting and thus may introduce artifacts into receptor binding assays.