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Immunochemical Characterisation of the Low‐Incidence Antigen, Dh a
Author(s) -
Spring F.A.
Publication year - 1991
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.1423-0410.1991.tb00930.x
Subject(s) - glycophorin , antigen , sialoglycoprotein , microbiology and biotechnology , epitope , trypsin , monoclonal antibody , sialidase , chemistry , biology , antibody , sialoglycoproteins , biochemistry , neuraminidase , enzyme , glycoprotein , immunology
. Immunoblotting with two examples of anti‐Dh a to the electrophoretically separated components of antigen‐positive membranes gave a positive reaction with a component of the same apparent Mr (40,000) as sialoglycoprotein β (SGP β, syn: glycoconnectin, glycophorin C). The Dh a antigenic determinant was sensitive to trypsin, but resistant to chymotrypsin and Endo F. By immunoblotting, one anti‐Dh a failed to react with sialidase‐treated Dh(a+) cells, whilst the other gave a positive result. In contrast, neither antibody agglutinated sialidase‐treated red cells. SGP β was precipitated from Dh(a+) and Dh(a‐) phenotype red cells by monoclonal anti‐β (NBTS/BRIC 10). SGP β from Dh(a+) but not from Dh(a‐) red cells was stained by immunoblotting with anti‐Dh a . These results assign the Dh a antigenic epitope to SGP β.