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Lack of Identity of the A Antigen and Concanavalin A Receptor on Bovine Erythrocytes; Implications for Membrane Structure 1
Author(s) -
OstrandRosenberg Suzanne
Publication year - 1976
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1976.tb02827.x
Subject(s) - trypsinization , concanavalin a , antigen , receptor , cell surface receptor , cell membrane , membrane , biology , lectin , epitope , microbiology and biotechnology , biochemistry , chemistry , trypsin , immunology , in vitro , enzyme
. Concanavalin A binding experiments on trypsinized and nontrypsinized bovine red cells strongly indicate that the con A receptor and the A antigen are molecularly independent cell surface entities. Untrypsinized bovine red cells are not agglutinated by con A, although such cells do bind the lectin. Trypsinization of A‐positive cells causes increased binding of anti‐A antibodies, accompanied by clustering of the A antigen sites on the membrane. Following trypsinization additional con A is also bound, but the con A receptors are not seen to aggregate in the membrane. This selective ligand‐induced antigen redistribution in the membrane suggests that mammalian red cell membranes are in a fluid state, and that the fluidity of membrane moieties can vary.