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Blood Group A Antigen in Human Erythrocytic Membranes and Membrane Fractions 1
Author(s) -
Kent S. P.,
McKibbin J. M.,
Boggio R.,
McKibbin J. B.
Publication year - 1977
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.1423-0410.1977.tb04463.x
Subject(s) - membrane , antigen , glycoprotein , glycolipid , red blood cell , biochemistry , hemagglutination , biology , membrane glycoproteins , chemistry , microbiology and biotechnology , immunology
. Erythrocytic membranes from blood group A individuals were assayed for A antigen using a quantitative hemagglutination inhibition technique. The membranes were then extracted for lipid and glycoprotein. Although some A antigen was usually found in the glycoprotein fraction, most of the activity was in the lipid fraction. The sum of A antigen activity in the lipid, glycoprotein, and membrane residue fractions only occasionally was equal to the A activity in the erythrocytic ghosts. However, when certain lipid preparations with little or no A antigen (enhancement factors) were added to the glycolipid fractions, the amount of A antigen demonstrated was usually greatly increased. Under these conditions, the sum of the fractions often was much greater than the A antigen demonstrated in erythrocytic membranes. This suggests that the organization or arrangement of A antigenic determinants in the red cell membrane may not always permit a stoichiometric reaction with anti‐A molecules.