title: Partial purification of dopamine D2 receptors using lectin affinity columns.
abstract: Dopamine D2 receptors, detected by [3H]spiperone binding, were solubilized from bovine caudate nucleus by cholate/sodium chloride and were found to bind to wheat germ agglutinin immobilized on agarose. Specific elution could be achieved with N-acetylglucosamine whereas other sugars tested were inactive in this regard. The eluted preparation was enriched in solubilized receptors about sevenfold. The pharmacological properties of the preparation were essentially unchanged by the lectin affinity purification procedure. The D2 dopamine receptor is therefore a glycoprotein.
authors.forename: W M
authors.initials: WM
authors.lastname: Abbott
authors.forename: P G
authors.initials: PG
authors.lastname: Strange
mesh_terms: D000117:Acetylglucosamine; D000818:Animals; D002417:Cattle; D002421:Caudate Nucleus / Q000032:analysis; D002846:Chromatography, Affinity; D006801:Humans; D037102:Lectins; D011954:Receptors, Dopamine / Q000302:isolation & purification* / Q000378:metabolism; D017448:Receptors, Dopamine D2; D012995:Solubility; D013134:Spiperone / Q000378:metabolism; D014909:Wheat Germ Agglutinins
chemical_list: D037102:Lectins; D011954:Receptors, Dopamine; D017448:Receptors, Dopamine D2; D014909:Wheat Germ Agglutinins; D013134:Spiperone; D000117:Acetylglucosamine