Mikulska J, Gorczyca W, Lisowski J
Department of Immunochemistry, Institute of Immunology and Experimental Therapy, Polish Academy of Science Czerska, Wroclaw, Poland.
Arch Immunol Ther Exp (Warsz). 1996;44(1):27-32.
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.
我们发现人血型糖蛋白和去唾液酸血型糖蛋白与人非免疫IgG相互作用。为了定量表征血型糖蛋白与IgG之间的相互作用，我们精心设计了一种直接固相放射免疫测定法。我们发现，在所使用的IgG浓度范围内，IgG的结合是可逆且可饱和的。血型糖蛋白结合的聚集免疫球蛋白量高于非聚集免疫球蛋白。非聚集人IgG的表观缔合常数为5.45±0.93×10⁵ M⁻¹，每1皮克血型糖蛋白结合1.13±0.78×10⁶个IgG分子。血型糖蛋白的结合主要发生在IgG的F(ab)2片段内。
