Photolabeling of brain membrane proteins by lysergic acid diethylamide

Under ultraviolet light, 3H-LSD forms an irreversible covalent bond with some proteins in bovine caudate membranes. The pattern of this photolabeling on gels differs from the general protein staining pattern, but it does not specifically target LSD binding sites linked to neurotransmitter receptors. Because photolabeling can also occur simply from prolonged exposure to room light, it may create artifacts in receptor binding assays.

Study at a glance

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.