title: Characterisation of Concanavalin A-binding glycoproteins from mouse splenic leukocytes by two-dimensional electrophoresis: preferential binding of incompletely glycosylated forms of H-2 antigen to the lectin.
abstract: Concanavalin A (Con A)section-binding proteins from mouse spleen leukocytes were characterised by two-dimensional electrophoresis of material precipitated, by Con A plus anti-Con A, from lysates of biosynthetically-labelled cells. Although most cell surface (iodinatable) proteins are known to bind Con A, some of the major Con A-binding proteins detected by immunoprecipitation, after a four-hour biosynthetic labelling period, are not iodinatable and are probably intracellular. Thus the major biosynthetically labelled Con A-binding species are: (i) a non-iodinatable, high molecular weight glycoprotein (C-145); (ii) intracellular precursors of secretory immunoglobulins (IgM and, probably, IgA); (iii) immature (not fully-sialylated) forms of H-2 D and K antigens; and (iv) Ia antigens. In the case of the H-2 antigens, (and possibly of other cell surface proteins) the selection of immature forms by Con A is not due to lack of biosynthetic labelling of mature products, but to preferential binding of Con A to incompletely glycosylated molecules.
mesh_terms: D000818:Animals; D000941:Antigens / Q000276:immunology; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D011232:Chemical Precipitation; D005260:Female; D006183:H-2 Antigens / Q000276:immunology*; D007123:Immunoelectrophoresis, Two-Dimensional; D066298:In Vitro Techniques; D007962:Leukocytes / Q000276:immunology*; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008970:Molecular Weight; D011952:Receptors, Concanavalin A / Q000276:immunology* / Q000302:isolation & purification; D013154:Spleen / Q000166:cytology* / Q000276:immunology
chemical_list: D000941:Antigens; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D006183:H-2 Antigens; C030659:K antigens; D011952:Receptors, Concanavalin A; C027774:concanavalin A-binding glycoproteins