Todorov D M, Wilkinson P C, White R G
Immunology. 1968 Jul;15(1):51-64.
A double layer immunofluorescence method was used to explore the affinity of immunoglobulins and immunoglobulin fragments for the mast cells of the mouse tongue. Human IgG but not IgA or IgM showed such an affinity as revealed by fluorescence of globulin attached to the mast cell surface and to the mast cell granules. This affinity was found also in isolated H(γ) chains but not in the light chains of IgG. After papain digestion, the Fab and Fc fragments obtained showed no affinity for mouse tongue mast cells though the 5S fragment obtained after pepsin digestion retained activity. The human immunoglobulin sub-class IgG lacks the ability to bind to mouse tongue mast cells. In guinea-pig serum, γ- but not γ-globulin showed an affinity for mouse tongue mast cells. It was suggested that a specific attachment site for mouse tongue mast cell surface receptors was present on the γ chain of human IgG and that this site was in a position susceptible to attck by papain hydrolysis.
采用双层免疫荧光法探究免疫球蛋白及其片段与小鼠舌部肥大细胞的亲和力。人IgG而非IgA或IgM表现出这种亲和力，这可通过附着于肥大细胞表面和肥大细胞颗粒的球蛋白荧光显示出来。在分离出的H(γ)链中也发现了这种亲和力，但在IgG的轻链中未发现。木瓜蛋白酶消化后，获得的Fab和Fc片段对小鼠舌部肥大细胞无亲和力，而胃蛋白酶消化后获得的5S片段仍保留活性。人免疫球蛋白亚类IgG缺乏与小鼠舌部肥大细胞结合的能力。在豚鼠血清中，γ球蛋白而非γ-球蛋白对小鼠舌部肥大细胞表现出亲和力。提示人IgG的γ链上存在小鼠舌部肥大细胞表面受体的特异性附着位点，且该位点易受木瓜蛋白酶水解攻击。
