title: Immunoprecipitation and partial characterization of diphtheria toxin-binding glycoproteins from surface of guinea pig cells.
abstract: 125I-Labeled membrane glycoproteins that specifically interact with diphtheria toxin and CRM197 protein--but not with diphtheria toxoid, fragment A of diphtheria toxin, or cholera toxin--were detected by use of the lactoperoxidase labeling technique followed by an immunoprecipitation system. These glycoproteins, which adhere to lentil lectin-Sepharose columns, are present on the surface of diphtheria toxin-sensitive guinea pig lymph node cells but are completely lacking on the surface of diphtheria toxin-resistant mouse L cells. The major 125I-labeled glycoprotein that interacts with diphtheria toxin exhibits anomalous behavior, characteristic of glycoproteins, when analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. This demonstration of the biochemical nature of specific diphtheria toxin binding membrane components raises the possibility that the detected components are diphtheria toxin receptors.
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D002772:Cholera Toxin / Q000378:metabolism; D004167:Diphtheria Toxin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006168:Guinea Pigs; D007158:Immunologic Techniques; D007739:L Cells / Q000378:metabolism; D008198:Lymph Nodes / Q000378:metabolism; D046911:Macromolecular Substances; D011955:Receptors, Drug / Q000378:metabolism*
chemical_list: D004167:Diphtheria Toxin; D006023:Glycoproteins; D046911:Macromolecular Substances; D011955:Receptors, Drug; D002772:Cholera Toxin