STUDIES ON THE IMMUNOGLOBULIN-G FC-FRAGMENT RECEPTOR FROM NEONATAL RAT SMALL-INTESTINE
STUDIES ON THE IMMUNOGLOBULIN-G FC-FRAGMENT RECEPTOR FROM NEONATAL RAT SMALL-INTESTINE
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DOI：
10.1042/bj1880009
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发表时间：
1980-01-01
影响因子：
4.1
通讯作者：
REES, AR
中科院分区：
文献类型：
--
作者：
WALLACE, KH;REES, AR
本文介绍了一种制备新生大鼠小肠刷状缘膜的方法，该方法是用酶法去除伴生多糖和细胞核。125I标记的Ig(免疫球蛋白)G和125I标记的Ig Fc片段与刷子边缘具有高度的特异性结合和较低的非特异性结合。F(Ab)~(‘2)片段不结合，表明Ig G的Fc片段存在特异性受体。受体系统是饱和的，用平衡法和动力学方法测定了与大鼠Ig G结合的亲和力(Ka)。比较了异种Ig G与人和牛的结合，结果表明人Ig G与大鼠Ig G在受体亲和力上非常相似。动力学结果与先前提出的配体诱导受体聚集模型一致。
A method for preparing this small-intestinal brush-border membrane of neonatal rats was described in which enzymic methods were used to remove associated polysaccharide and cell nuclei. 125I-labeled Ig(immunoglobulin)G and 125I-labeled IgG Fc fragment had high specific binding and low non-specific binding to brush borders prepared in this way. F(ab)''2 fragment did not bind, indicating the existence of a specific receptor for the Fc fragment of IgG. The receptor system was saturable, and the affinity (KA) for the binding of rat IgG was determined by equilibrium and kinetic methods. Binding of heterologous IgG species (human and bovine) was compared and demonstrated close similarity between human IgG and rat IgG in their receptor affinities. Kinetic results were presented that are consistent with previously proposed models of ligand-induced receptor aggregation.