Characterization of a 140Kd cell surface glycoprotein involved in myoblast adhesion.
Two monoclonal antibodies that cause changes in the morphology of cultured chick myogenic cells have been described previously [8]. In this paper, these antibodies are shown to interact with the same 140Kd protein. The 140Kd protein has been further characterized as a cell-surface glycoprotein by lactoperoxidase-catalyzed iodinations and lectin affinity chromatography. The protein is resistant to digestion by trypsin and collagenase and has been shown to be unrelated to fibronectin by immunoprecipitation studies and by peptide mapping. A second protein, of approximately 170Kd MW, is also immunoprecipitated by the monoclonal antibodies. This protein is probably unrelated to the 140Kd protein since the peptide maps are quite distinct.
D000818:Animals; D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000276:immunology; D002448:Cell Adhesion; D002642:Chick Embryo; D005347:Fibroblasts / Q000032:analysis / Q000166:cytology; D006023:Glycoproteins / Q000032:analysis* / Q000276:immunology; D007163:Immunosorbent Techniques; D008565:Membrane Proteins / Q000032:analysis* / Q000276:immunology; D009132:Muscles / Q000032:analysis* / Q000166:cytology / Q000196:embryology; D014357:Trypsin / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D006023:Glycoproteins; D008565:Membrane Proteins; D014357:Trypsin