PARTIAL-PURIFICATION OF RHO(D) ANTIGEN FROM RH-POSITIVE AND RH-NEGATIVE ERYTHROCYTES

A rapid method is described for partial purification of Rh(o)(D) antigen from sodium deoxycholate-solubilized erythrocyte membranes by affinity chromatography on a column coupled with anti-Rh(o)(D) IgG. The Rh(o)(D) antigen is a low molecular weight membrane protein that comigrates with the lipid zone of erythrocytes during sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Similar quantities of Rh(o)(D) antigen were present in Rh positive and negative erythrocytes. However, in the latter erythrocytes the antigen may not be exposed to the external cell surface, explaining why these cells are not agglutinated by anti-Rh(o)(D) antiserum. LW antigen was also present in the fraction containing Rh(o)(D) antigen. The genetic implications of these findings are discussed.