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An Erythrocyte Glycoprotein of Apparent M r 60,000 Expresses the Sc1 and Sc2 Antigens
Author(s) -
Spring F. A.,
Herron R.,
Rowe G.
Publication year - 1990
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1990.tb02074.x
Subject(s) - antigen , glycoprotein , pronase , microbiology and biotechnology , glycan , membrane glycoproteins , biology , pan t antigens , chemistry , immunology , biochemistry , antibody , trypsin , monoclonal antibody , enzyme
. Immunoblotting with human anti‐Sc1 and anti‐Sc2 locates the Sc1 and Sc2 antigens to an erythrocyte membrane glycoprotein of apparent M r 60,000. The antigens are destroyed by pronase, and require intact disulphide bonds for expression. A proportion of the molecules carrying the Sc1 and Sc2 antigens are associated with red cell cytoskeleton preparations. Treatment of intact cells with an Endo F preparation resulted in the loss of the Sc2 antigen but not the Sc1 antigen, suggesting that the Sc2 antigen is dependent on the presence of one or more complex N‐glycans for its expression.