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Scientific article
English

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

Published inMolecular immunology, vol. 20, no. 4, p. 491-497
Publication date1983
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
Affiliation Not a UNIGE publication
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
Identifiers
ISSN of the journal0161-5890
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