兔免疫球蛋白G及其酶解片段与同源腹腔巨噬细胞的结合
The binding of rabbit IgG and its enzymatically derived fragments to homologous peritoneal macrophages.
作者信息
Ganczakowski M, Leslie R G
出版信息
Immunology. 1979 Mar;36(3):487-94.
Rabbit IgG and its Fab, Fc and pFc' fragments, prepared by papain or peptic digestion, were assayed for binding to homologous peritoneal macrophages. The binding affinity of IgG for the peritoneal macrophages (Ka = 5.9 +/- 1.6 x 10(5) L/M) was comparable to that recorded with alveolar macrophages (7.6 +/- 1.8 x 10(5) L/M, Arend & Mannik, 1973) but the number of receptor sites per peritoneal cell (4.6 +/- 2.1 x10(6)) was about four-fold greater than on the latter. Of the fragments, only Fc bound to macrophages with an affinity comparable to intact IgG; pFc' bound weakly and Fab was totally inactive. These data, taken with a recent study involving rabbit IgG and guinea-pig macrophages (Ovary, Saluk, Quijada & Lamm, 1976), indicate that the primary IgG binding site for macrophages is located in the C gamma 2 domain.
通过木瓜蛋白酶或胃蛋白酶消化制备的兔免疫球蛋白（IgG）及其Fab、Fc和pFc'片段，检测其与同源腹膜巨噬细胞的结合情况。IgG与腹膜巨噬细胞的结合亲和力（Ka = 5.9 +/- 1.6 x 10(5) L/M）与肺泡巨噬细胞的记录值相当（7.6 +/- 1.8 x 10(5) L/M，Arend和Mannik，1973年），但每个腹膜细胞的受体位点数量（4.6 +/- 2.1 x10(6)）约为肺泡巨噬细胞的四倍。在这些片段中，只有Fc与巨噬细胞的结合亲和力与完整IgG相当；pFc'结合较弱，而Fab完全无活性。这些数据，结合最近一项涉及兔IgG和豚鼠巨噬细胞的研究（Ovary、Saluk、Quijada和Lamm，1976年），表明巨噬细胞的主要IgG结合位点位于Cγ2结构域。
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