title: Contamination of serotonin-2 binding sites by an alpha-1 adrenergic component in assays with (3H)spiperone.
abstract: (3H)Spiperone binds to two sites in mouse cortical membranes. These binding sites are discriminated by methysergide and prazosin, but not by butaclamol, lysergic acid diethylamide, or ketanserin. One of these sites is serotonergic in nature and is the authentic S-2 binding site. The other component is adrenergic and corresponds to the alpha-1 adrenoreceptor. This alpha-1 component may be present in other S-2 binding assays using (3H)spiperone, or (3H)ketanserin. No (3H)spiperone binding to dopaminergic D-2 sites was found in mouse cortex. Methods of avoiding alpha-1 contamination of S-2 binding assays are suggested.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002090:Butyrophenones / Q000378:metabolism*; D002540:Cerebral Cortex / Q000378:metabolism; D066298:In Vitro Techniques; D008784:Methysergide / Q000494:pharmacology; D051379:Mice; D011224:Prazosin / Q000494:pharmacology; D011942:Receptors, Adrenergic, alpha / Q000032:analysis*; D011954:Receptors, Dopamine / Q000378:metabolism; D011985:Receptors, Serotonin / Q000032:analysis*; D013134:Spiperone / Q000378:metabolism*; D014316:Tritium
chemical_list: D002090:Butyrophenones; D011942:Receptors, Adrenergic, alpha; D011954:Receptors, Dopamine; D011985:Receptors, Serotonin; D014316:Tritium; D013134:Spiperone; D011224:Prazosin; D008784:Methysergide