Glycoprotein properties of benzodiazepine receptors from calf cerebral cortex.
Several lectins (concanavalin A, wheat germ agglutinin, wax bean agglutinin, and phytohemagglutinin) induce aggregation and precipitation of deoxycholate-solubilized benzodiazepine receptors from calf cerebral cortex. These receptors were also retained on columns of immobilized lectins. Photoaffinity labeling of the soluble benzodiazephine receptors prevented their interaction with lectins. Periodate treatment caused inactivation of benzodiazepine receptors which was partially prevented by diazepam and/or gamma-aminobutyric acid. The possible association of the drug-binding site and the carbohydrate moiety is discussed.
D000818:Animals; D002417:Cattle; D002540:Cerebral Cortex / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D003864:Depression, Chemical; D005445:Flunitrazepam / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis*; D037102:Lectins / Q000494:pharmacology; D010504:Periodic Acid / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000032:analysis* / Q000187:drug effects; D011963:Receptors, GABA-A
D006023:Glycoproteins; D037102:Lectins; D011956:Receptors, Cell Surface; D011963:Receptors, GABA-A; D010504:Periodic Acid; D005445:Flunitrazepam; C009288:metaperiodate