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

Transfusion. Mar-Apr 1990;30(3):222-5. doi: 10.1046/j.1537-2995.1990.30390194341.x.


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 Mr 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology*
  • Erythrocyte Membrane / analysis*
  • Glycoproteins / blood*
  • Humans
  • Immunoblotting
  • Mice
  • Rh-Hr Blood-Group System*


  • Antibodies, Monoclonal
  • Glycoproteins
  • Rh-Hr Blood-Group System