Evidence for erythrocyte membrane glycoproteins being carriers of blood-group P1 determinants.
The contribution of different membrane constituents to the bloodgroup P1 activity of human erythrocytes was investigated. Pronase digestion of native red cell stroma or partition between butanol and water had no serologically detectable effect, whereas pronase-treatment of previously butanol-extracted membranes liberated virtually all blood-group P1 determinants from the ghosts. On Laemmli gels, all P1 activity was found in the band 4.5 region. Thus it is concluded that, in addition to the well-documented P1 glycolipid, also membrane glycoproteins are carriers of blood-group P1 determinants.
D001789:Blood Group Antigens / Q000276:immunology*; D001798:Blood Proteins / Q000276:immunology*; D000939:Epitopes / Q000032:analysis*; D004910:Erythrocyte Membrane / Q000276:immunology*; D004912:Erythrocytes / Q000276:immunology*; D006023:Glycoproteins / Q000276:immunology*; D006385:Hemagglutination Inhibition Tests; D006386:Hemagglutination Tests; D006801:Humans; D010127:P Blood-Group System / Q000276:immunology*
D001789:Blood Group Antigens; D001798:Blood Proteins; D000939:Epitopes; D006023:Glycoproteins; D010127:P Blood-Group System