Partial purification of Rho (D) antigen from Rh positive and negative erythrocytes.

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