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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
Authors
Pink, J. R.
Hoessli, Daniel
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 Animals — Antigens/immunology — Antigens, Bacterial — Antigens, Surface — Chemical Precipitation — Female — H-2 Antigens/ immunology — Immunoelectrophoresis, Two-Dimensional — Leukocytes/ immunology — Male — Mice — Mice, Inbred Strains — Molecular Weight — Receptors, Concanavalin A/ immunology/isolation & purification — Spleen/ cytology/immunology
Identifiers
PMID: 6865960
Full text
Other version: http://www.nature.com/nature/journal/v283/n5747/pdf/283576a0.pdf
Citation
(ISO format) 		PINK, J. R. et al. 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. In: Molecular Immunology, 1983, vol. 20, n° 4, p. 491-497. https://archive-ouverte.unige.ch/unige:10956

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Deposited on : 2010-08-26

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