Scientific Article
previous document  unige:10956  next document
add to browser collection

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

Pink, J. R.
Tartakoff, A.
Hooghe, R.
Published in Molecular Immunology. 1983, vol. 20, no. 4, p. 491-497
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.
Keywords AnimalsAntigens/immunologyAntigens, BacterialAntigens, SurfaceChemical PrecipitationFemaleH-2 Antigens/ immunologyImmunoelectrophoresis, Two-DimensionalLeukocytes/ immunologyMaleMiceMice, Inbred StrainsMolecular WeightReceptors, Concanavalin A/ immunology/isolation & purificationSpleen/ cytology/immunology
Stable URL
Full text
PMID: 6865960
139 hits and 0 download since 2010-08-26
Export document
Format :
Citation style :