Abbas A K, Unanue E R
J Immunol. 1975 Dec;115(6):1665-71.
Receptors for the Fc portion of immunoglobulin (Ig) molecules have been detected on mouse B lymphocytes by an immunofluorescence technique, employing immune complexes of fluorescein-conjugated KLH and rabbit anti-KLH antibody. At 37 degrees C, membrane-bound complexes rapidly undergo capping and clearing from the surface. Modulation of Fc receptors does not alter the amount of distribution of surface Ig, indicating that these two molecules are independent moieties. However, capping of surface Ig by intact or pepsin-digested anti-Ig antibody leads to co-capping of Fc receptors. These results suggest that ligand binding to surface Ig induces some alteration which allows the Ig to enter into an association with Fc receptors.
利用异硫氰酸荧光素偶联的钥孔戚血蓝蛋白(KLH)与兔抗KLH抗体的免疫复合物,通过免疫荧光技术在小鼠B淋巴细胞上检测到了免疫球蛋白(Ig)分子Fc段的受体。在37℃时,膜结合复合物迅速发生帽化并从表面清除。Fc受体的调节不会改变表面Ig的数量或分布,表明这两种分子是独立的部分。然而,完整的或经胃蛋白酶消化的抗Ig抗体对表面Ig的帽化会导致Fc受体的共帽化。这些结果表明,配体与表面Ig的结合会引起一些改变,使Ig能够与Fc受体结合。