Blood-group serology of fractions obtained from the human erythrocyte membrane.

Abstract

The activity of a large number of human erythrocyte antigens was monitored through a procedure which fractionates the erythrocyte membrane proteins. A significant amount of the erythrocyte “ghost” protein could be removed by aqueous extractants without affecting the activity of any antigen. Subsequent extraction of the residual “ghosts” with pyridine solution resulted in a separation of blood group M, N and Pr activities from blood group A, P1, P and I activities. A number of antigens including c, C, D, k, Kpb, Jka and Fya were labile to this treatment. Gel filtration in the presence of detergent showed that the MN and Pr activity was associated with the erythrocyte sialoglycoprotein. In agreement with Whittemore et al. (1969) two types of blood‐group‐A antigen could be distinguished on the basis of their partition properties on butanol extraction. Type OS‐A antigen can be extracted into butanol, while type WS‐A antigen is retained in the aqueous phase. The characteristics of blood‐group‐P antigen were similar to that of type OS‐A antigen, while blood‐group‐I antigen and type WS‐A antigen showed similar behaviour.