Murine monoclonal antibody MB‐2D10 recognizes Rh‐related glycoproteins in the human red cell membrane

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Abstract
The human red cell membrane components reacting with monoclonal antibody MB‐2D10 were examined by immunoblotting. The antibody bound to a diffusely staining band extending from M, 30,000 up to the high‐molecular‐weight region of the gel in normal membranes and in Rhnull U+ membranes, but not in Rhnull U‐ membranes. Treatment of normal red cells with an endoglycosidase F‐containing preparation destroyed the epitope recognized by MB‐2D10. The reactivity of the antibody with purified preparations of Rh‐related glycoproteins D30 polypeptide, D50 polypeptide, R6A32 polypeptide, and R6A45 polypeptide was also examined. Only the purified R6A45 and D50 components reacted with MB‐2D10. These results show that MB‐2D10 recognizes a carbohydrate‐dependent epitope on the R6A45 and D50 group of Rh‐related polypeptides. The results also suggest the possibility that the U antigen arises from interaction between glycophorin B and the Rh‐related components D50 and R6A45.