Abstract
An antibody-lectin sandwich enzyme immunoassay for analysis of altered sugar chains in serum transferrin of patients with hepatoma was developed. Anti-transferrin lgGcoated polystyrene beads incubated with neuraminidase-treated serum samples were reacted with peroxidase (POD)-conjugated lectins such as ricinus communis agglutinin (RCA), lens culinaris agglutinin (LCA), phytohemagglutinin-E4 (EPHA), and phytohemagglutin-L4 (LPHA). The amounts of lectins bound to the sugar chains in transferrin were determined by measurement of the POD activities. The LCA/RCA, EPHA/RCA, and LPHA/RCA POD activity ratios were increased significantly in sera from patients with hepatoma in comparison with those in healthy individuals. These results indicated that fucosylation at the reduced end of the N-acetylglucosamine residue, bisecting N-acetylglucosamine at the trimannosyl core, and highly-branched complex-type sugar chains were increased in serum transferrin of patients with hepatoma.
