Other version: http://www.nature.com/nature/journal/v283/n5747/pdf/283576a0.pdf
Highlights
![]() |
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 | ||
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 | ||
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. doi: 10.1016/0161-5890(83)90030-5 https://archive-ouverte.unige.ch/unige:10956 |