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Characterization of the epitope recognized by a monoclonal antibody highly specific for blood group M antigen
Author(s) -
Jaskiewicz E.,
Moulds J.J.,
Kraemer K.,
Goldstein A.S.,
Lisowska E.
Publication year - 1990
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1990.30390194343.x
Subject(s) - epitope , glycophorin , antigen , monoclonal antibody , antibody , microbiology and biotechnology , sialic acid , hemagglutination , chemistry , red blood cell , serine , glycoprotein , biochemistry , enzyme , biology , immunology
The mouse monoclonal antibody M2A1 of IgG1 class, which is highly specific for blood group M antigen, was obtained and characterized by means of hemagglutination, enzyme‐linked immunosorbent assay, immunoblotting, and inhibition assays. The use of modified M glycoprotein preparations for inhibition tests and of variant M C N and Henshaw red cell membranes for immunoblotting showed that M2A1 recognized an epitope including the NH 2 ‐terminal serine and sialic acid residues of glycophorin A, whereas the fifth glycine residue was not involved. The reactivity of the antibody with M antigen was distinctly dependent on ionic strength and pH; the optimum was at pH 8 to 9. The α‐amino group of terminal serine residue was not necessary for the reaction with M2A1 antibody, and the results obtained suggested that the positive charge of this group contributed to decreasing antigen‐antibody reactions at pH below 8. The reaction of the antibody with blood group N antigen was not detectable in any of the assays used.