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Radioimmunoassay Studies of the Cross‐reacting Antibody of Human Group O Sera
Author(s) -
Holburn A. M.
Publication year - 1976
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1976.tb00963.x
Subject(s) - radioimmunoassay , antibody , chemistry , antiserum , glycoprotein , antigen , monosaccharide , microbiology and biotechnology , biochemistry , biology , immunology
Cross‐reacting antibody was obtained from three recently stimulated group O donors. The biological reactions of cross‐reacting antibody were investigated by a study of the binding characteristics of 125 I‐labelled purified IgG fractions with red cells and by the reactions of whole antiserum or eluates with 125 I‐labelled blood group glycoproteins. The bulk of cross‐reacting antibody activity is restricted to the IgG fraction. Experiments with 125 I‐labelled IgG and with the radioimmunoassay system revealed that cross‐reacting antibody has a higher binding constant than specific anti‐A or anti‐B. In the radioimmunoassay system complete inhibition of cross‐reacting antibody was obtained either with D‐galactose or with N‐acetyl‐D‐galactosamine, but the same concentrations of monosaccharides gave only partial inhibition of specific anti‐A and anti‐B antibodies. The results indicate that cross‐reacting antibody binds to a smaller determinant than specific antibody. Investigations with other monosaccharides did not, however, reveal a common inhibitory structure. The ability of cross‐reacting antibody to bind to both group A and B antigens may, therefore, be a property of a ‘Polyfunctional’ antibody binding site.