Interaction of dihydrotetrabenazine binding activity with immobilized lectins.
High-affinity dihydrotetrabenazine binding activity was solubilized by treatment of crude bovine striatal synaptosomes with cholate and incubated with lectins immobilized on sepharose. Both concanavalin A and wheat germ lectin sepharose removed dihydrotetrabenazine binding activity from the cholate extract, and this removal was prevented by inclusion of the appropriate hapten sugars. These results imply that the dihydrotetrabenazine binding subunit of the synaptic vesicle catecholamine/serotonin (5-HT) transporter, or a vesicle component tightly associated with it, is glycosylated.
Department of Pharmacology, Indiana University School of Medicine, Bloomington 47405.
M S
MS
Vincent
J A
JA
Near
D000327:Adsorption; D000818:Animals; D002417:Cattle; D003208:Concanavalin A / Q000378:metabolism; D003342:Corpus Striatum / Q000378:metabolism; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism*; D013574:Synaptosomes / Q000378:metabolism*; D013747:Tetrabenazine / Q000031:analogs & derivatives* / Q000378:metabolism; D014909:Wheat Germ Agglutinins / Q000378:metabolism
D037102:Lectins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A; C032811:dihydrotetrabenazine; D013747:Tetrabenazine