Interaction of Human Erythrocyte Glycophorin with Immunoglobulins G
JOANNA MIKULSKA, WOJCIECH GORCZYCA and JÓZEF LISOWSKI
Abstract. We have found that human glycophorin and asialoglycophorin interacted with human non-immune IgG. To characterize quantitatively the interaction between glycophorin and IgG we elaborated a direct solid-phase radioimmunoassay. We showed that the binding of IgG was reversible and saturable within the range of IgG concentrations used. Glycophorin bound higher amounts of aggregated than non-aggrega- ted immunoglobulins. The apparent association constant for non-aggregated human IgG was 5.45 ± 0.93 x 105 M-1 and 1.13 ± 0.78 x 106 IgG molecules were bound per 1 picogram of the glycophorin. The binding of glycophorin occurs within the F (ab')2 fragment of IgG, mainly.
Keywords: erythrocyte; glycophorin; receptors; ligand-receptor interactions; immunoglobulin G.ulin G.