Interaction of human erythrocyte glycophorin with immunoglobulins G.
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-aggregated immunoglobulins. The apparent association constant for non-aggregated human IgG was 5.45 +/- 0.93 x 10(5) M-1 and 1.13 +/- 0.78 x 10(6) IgG molecules were bound per 1 picogram of the glycophorin. The binding of glycophorin occurs within the F(ab)2 fragment of IgG, mainly.
Mikulska
J
J
Department of Immunochemistry, Institute of Immunology and Experimental Therapy, Polish Academy of Science Czerska, Wroclaw, Poland.
Gorczyca
W
W
Lisowski
J
J
D001212:Asialoglycoproteins / Q000378:metabolism*; D004910:Erythrocyte Membrane; D006021:Glycophorins / Q000378:metabolism*; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011485:Protein Binding; D011863:Radioimmunoassay; D011956:Receptors, Cell Surface / Q000378:metabolism
D001212:Asialoglycoproteins; D006021:Glycophorins; D007074:Immunoglobulin G; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; C026503:asialoglycophorin