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- W2009376439 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." @default.
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- W2009376439 date "1990-03-01" @default.
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- W2009376439 title "Murine monoclonal antibody MB-2D10 recognizes Rh-related glycoproteins in the human red cell membrane" @default.
- W2009376439 doi "https://doi.org/10.1046/j.1537-2995.1990.30390194341.x" @default.
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