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Murine monoclonal antibody MB‐2D10 recognizes Rh‐related glycoproteins in the human red cell membrane
Author(s) -
Mallinson G.,
Anstee D.J.,
Avent N.D.,
Ridgwell K.,
Tanner M.J.A.,
Daniels G.L.,
Tippett P.,
Borne A.E.G.
Publication year - 1990
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1990.30390194341.x
Subject(s) - epitope , glycophorin , glycoprotein , monoclonal antibody , microbiology and biotechnology , antibody , antigen , chemistry , membrane glycoproteins , endoglycosidase , biochemistry , membrane , biology , immunology
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 Rh null U+ membranes, but not in Rh null 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 D 30 polypeptide, D 50 polypeptide, R6A 32 polypeptide, and R6A 45 polypeptide was also examined. Only the purified R6A 45 and D 50 components reacted with MB‐2D10. These results show that MB‐2D10 recognizes a carbohydrate‐dependent epitope on the R6A 45 and D 50 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 D 50 and R6A 45 .