Abstract
Ghosts were prepared from erythrocytes positive for the rare blood group antigen Pt^a. Immunoblotting of the solubilised ghosts with anti-Pt^a located the antigen on a band with an M(r)r of 31,600, about 1,100 higher than that of sialoglycoprotein γ. Binding to the same band was also observed when cytoskeleton preparations from Pt(a+) erythrocytes were immunoblotted with the antibody. Haemagglutination and immunoblotting experiments were consistent in demonstrating that the Pt^a antigen is not inactivated by treatment of intact erythrocytes with neuraminidase or trypsin but is destroyed by treatment with α-chymotrypsin, papain or pronase. The data indicate that the Pt^a antigen is carried on a ‘new’ erythrocyte membrane protein.
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