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Evidence that the c, D and E epitopes of the human Rh blood group system are on separate polypeptide molecules
N C Hughes-Jones1, C Bloy, B Gorick
1Unité INSERM U76, Institut National de Transfusion Sanguine, Paris, France.
The distribution of the epitopes, c, D, E and G of the human Rh system on red cells has been investigated using both 125I-labelled and fluorescently-labelled MAbs. There is a very wide range in the density of each epitope on individual red cells and the numbers of c, D and E epitopes on each cell are independent of each other. These observations taken together with the finding that there is no steric hindrance to binding between the antibodies, anti-c, anti-D and anti-E indicate that these epitopes are on separate Rh polypeptide molecules. The observations are taken to indicate that the total amount of Rh polypeptide on a single red cell is constant but that there is considerable heterogeneity between cells in the amount of each separate polypeptide carrying the different epitopes. In contrast, there was a mutual inhibition of binding of anti-G and anti-D monoclonals and direct positive correlation between the number of G and D sites on individual cells, indicating that the G and D epitopes are probably on the same Rh polypeptide.
The distribution of the epitopes, c, D, E and G of the human Rh system on red cells has been investigated using both 125I-labelled and fluorescently-labelled MAbs. There is a very wide range in the density of each epitope on individual red cells and the numbers of c, D and E epitopes on each cell are independent of each other. These observations taken together with the finding that there is no steric hindrance to binding between the antibodies, anti-c, anti-D and anti-E indicate that these epitopes are on separate Rh polypeptide molecules. The observations are taken to indicate that the total amount of Rh polypeptide on a single red cell is constant but that there is considerable heterogeneity between cells in the amount of each separate polypeptide carrying the different epitopes. In contrast, there was a mutual inhibition of binding of anti-G and anti-D monoclonals and direct positive correlation between the number of G and D sites on individual cells, indicating that the G and D epitopes are probably on the same Rh polypeptide.