Abstract
Antibody to the carbohydrate moiety of T antigen was developed. The synthetic antigen (Galβ1→3 GalNAcα1→OC6H4 N=N-BSA) was prepared by coupling the diazonium salt of the disaccharide derivative Galβl→3 GalNAcαrarr;OC6H H4NH2 (o) with bovine serum albumin. Specificity of the antibody produced was examined with structurally related synthetic saccharides using the enzyme immunoassay technique. The presence of a glycosyl group at 0-6 of either the Gal or the GalNAc residue of the disaccharide Galβl→3 GalNAc did not prevent binding of the antisera to the saccharide moiety. However, the antisera did not bind either the trisaccharide moiety NeuAc2→3 Galβrarr;3 GalNAcαl→OC6H4NO2 (O) or GlcNAcβl→3 Galβl→3 GalNAc α OBn. These observations indicate that antibody approach to the antigen is to the 0-3 side of the terminal galactose in the disaccharide Galβl→3 GalNAc. We have also observed that the antibody prefers Galβl→3 GalNAcα1→ to Galβl→3 GalNAcβl → disaccharide derivatives in its binding capacity., The antibody was found to bind natural T antigen present on neuraminidase-treated red blood cells and, by immunohistochemical analysis, it was found to bind to naturally ocurring T antigen on breast tumor cells.
| Original language | English |
|---|---|
| Pages (from-to) | 151-163 |
| Number of pages | 13 |
| Journal | Immunological Investigations |
| Volume | 16 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1987 |
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