Lentil-lectin affinity chromatography of surface glycoproteins and the receptor for IgE from rat basophilic leukemia cells.
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).
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
D006023:Glycoproteins; D037102:Lectins; D008766:Methylmannosides; D007073:Immunoglobulin E