title: Monoclonal antibody detects carbohydrate microheterogeneity on the murine cell adhesion molecule L1.
abstract: The cell surface glycoprotein L1 is involved in neural cell interactions and shares with other adhesion molecules, i.e. the neural cell adhesion molecule N-CAM, the myelin-associated glycoprotein MAG and the J1 glycoproteins, an unusual carbohydrate structure designated L2/HNK-1. Recent evidence suggests that the L2/HNK-1 carbohydrate participates in adhesion. Since indirect evidence indicated that the L2/HNK-1 carbohydrate is not present on all molecules within a particular species of glycoproteins, it seemed pertinent to investigate this more directly by sequential immunoprecipitations. Here we show that the L2/HNK-1 epitope appears to be present on 35% of the L1 glycoproteins isolated from mouse brain. The epitope is restricted to the proteolytic fragment of L1 at the aminoterminal, extracellular domain in that it is detectable on L1-200 and L1-140, but absent from L1-80 and L1-50.
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000032:analysis*; D001923:Brain Chemistry; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules; D000939:Epitopes / Q000032:analysis; D007118:Immunoassay; D008562:Membrane Glycoproteins / Q000032:analysis*; D051379:Mice
chemical_list: D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D015815:Cell Adhesion Molecules; D000939:Epitopes; D008562:Membrane Glycoproteins