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
- 1 April 1983
- journal article
- research article
- Published by Elsevier in Molecular Immunology
- Vol. 20 (4) , 491-497
- https://doi.org/10.1016/0161-5890(83)90030-5
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Uniformity of Glycans within Molecular Variants of αl‐Protease Inhibitor with Distinct Affinity for Concanavalin AEuropean Journal of Biochemistry, 1982
- Glycan uniformity within molecular variants of transferrin with distinct affinity for concanavalin ABiochemical and Biophysical Research Communications, 1982
- Intracellular transport of lymphoid surface glycoproteinsJournal of Molecular Biology, 1981
- Aberrant Ae (E beta) Ia polypeptide chain in H-2g2 haplotype mice. Possible result of an intragenic recombination or mutation.The Journal of Experimental Medicine, 1980
- Isolation, characterization and amino acid sequence studies of the cyanogen bromide fragments of the H‐2 Dd glycoproteinEuropean Journal of Immunology, 1980
- Interaction of lectins with human T lymphocytes mitogenic properties, inhibitory effects, binding to the cell membrane and to isolated surface glycopeptidesEuropean Journal of Immunology, 1980
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Analysis of H-2 and Ia molecules by two-dimensional gel electrophoresis.The Journal of Experimental Medicine, 1977
- Glycoproteins of murine thymocyte and splenocyte surface membranes; binding to Concanavalin A and recognition by heterologous antilymphocyte serumImmunochemistry, 1976
- CONCANAVALIN A BINDING PROTEINS OF LYMPHOID CELL SURFACEThe Journal of Experimental Medicine, 1974