Hemmings W A, Williams E W
Gut. 1978 Aug;19(8):715-23. doi: 10.1136/gut.19.8.715.
Ferritin or tritium labelled immunoglobulin G may, by electron microscopy, be demonstrated entering, within, and leaving the epithelial cells. Quantitative studies using various proteins labelled with radioiodine show that large amounts of protein bound radioactivity may be demonstrated in the tissues after feeding the labelled protein to adult rats by stomach tube. The molecular size of this material as determined by sugar gradient ultracentrifugation of tissue extracts ranges when IgG is fed from 50,000-20,000 Daltons. The material retains its ability to react as antigen with antisera specific to the original molecule: precipitation reactions may be obtained in gels and quantitative studies show that cnosiderable amounts of the protein-bound radioactivity are still specifically precipitable. Such studies have been carried out with alpha-gliadin as well as bovine IgG. At 100 days old rats may absorb as much as 40% of a dose of bovine IgG in the form of these large molecular breakdown products.
通过电子显微镜可证实,铁蛋白或氚标记的免疫球蛋白G进入、存在于并离开上皮细胞。使用各种放射性碘标记蛋白质的定量研究表明,通过胃管给成年大鼠喂食标记蛋白质后,在组织中可显示大量与蛋白质结合的放射性。当喂食IgG时,通过组织提取物的糖梯度超速离心法测定,这种物质的分子大小范围为50,000 - 20,000道尔顿。该物质保留了作为抗原与针对原始分子的抗血清发生反应的能力:在凝胶中可获得沉淀反应,定量研究表明,相当数量的与蛋白质结合的放射性仍可被特异性沉淀。已用α - 麦醇溶蛋白以及牛IgG进行了此类研究。100日龄的大鼠可能以这些大分子分解产物的形式吸收高达40%剂量的牛IgG。