Hardin J A, Nakaoka K K, Carboni J M
Proc Natl Acad Sci U S A. 1979 Feb;76(2):912-4. doi: 10.1073/pnas.76.2.912.
Radioiodinated IgM isolated from a patient with Waldenström macroglobulinemia binds with high avidity (apparent Ka = 2.5 x 10(9) M-1) to freshly isolated human peripheral blood lymphocytes. Binding occurred through the Fc region of the molecule and involved a receptor specific for immunoglobulins of the IgM class. The avidity and specificity of this binding are consistent with a biologic role for IgM receptors on lymphocytes.
从一名华氏巨球蛋白血症患者体内分离出的放射性碘化IgM,能以高亲和力(表观解离常数Ka = 2.5 x 10⁹ M⁻¹)与新鲜分离的人外周血淋巴细胞结合。这种结合是通过该分子的Fc区域发生的,并且涉及一种对IgM类免疫球蛋白具有特异性的受体。这种结合的亲和力和特异性与淋巴细胞上IgM受体的生物学作用是一致的。