ABO(H) blood group antigens of the human erythrocyte membrane:
Contribution of glycoprotein and glycolipid
Narendra G. Mehta
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Abstract
Formaldehyde-fixed human erythrocytes were extracted with sodium
dodecyl sulfate and with three other solvent systems, at least two of
which are known to remove glycolipids quantitatively. The extracted cells
possessed the ability to absorb the ABO blood group-specific antibody at
about onethird the level of unextracted cells. Treatment of fresh cells with
pronase also reduced the ability of the cells to absorb the antibody,
further supporting the presence of ABO blood group active glycoprotein
in the membrane. Trypsinization of red cells, while removing PAS-1 and
partly PAS-2, did not lead to any decrease in the activity. Papainization
also did not diminish the activity, although PAS-1, PAS-2, and PAS-3
were removed from the cells. Thus, both glycolipid and glycoprotein
contribute to ABO antigens of erythrocytes. Also, none of the three major
glycoproteins of the membrane bears this activity