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.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Pink JR,Hoessli D,Tartakoff A,Hooghe R

doi

10.1016/0161-5890(83)90030-5

subject

Has Abstract

pub_date

1983-04-01 00:00:00

pages

491-7

issue

4

eissn

0161-5890

issn

1872-9142

journal_volume

20

pub_type

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