title: Lentil-lectin affinity chromatography of surface glycoproteins and the receptor for IgE from rat basophilic leukemia cells.
abstract: Surface proteins and glycoproteins of RBL cells were labelled enzymatically with 125I and then solubilized with Nonidet P-40. Analysis by polyacrylamide-gel electrophoresis in SDS on 10% gel revealed 10 distinctive peaks ranging in molecular weights from 17,000 to 200,000 daltons. Mainly components of higher molecular weights were bound by lentil-lectin Sepharose and could be eluted with alpha-methyl mannoside. The receptor for IgE was clearly shown to bind to the lentil-lectin. A second cell surface component which previously had been shown to bind to IgE-Sepharose as well, was found to bind only slightly to lentil-lectin. Thus, it can be concluded that the receptor for IgE is a glycoprotein with mannose and/or N-acetylglucosamine in the carbohydrate moiety(s).
mesh_terms: D000818:Animals; D001491:Basophils; D001666:Binding Sites, Antibody; D002469:Cell Separation; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000276:immunology*; D007073:Immunoglobulin E; D037102:Lectins / Q000494:pharmacology*; D007938:Leukemia / Q000276:immunology; D008766:Methylmannosides / Q000494:pharmacology; D008970:Molecular Weight; D051381:Rats
chemical_list: D006023:Glycoproteins; D037102:Lectins; D008766:Methylmannosides; D007073:Immunoglobulin E