Escribano M J, Haddada H, de Vaux Saint Cyr C
J Immunol Methods. 1982;52(1):63-72. doi: 10.1016/0022-1759(82)90350-7.
The isolation of hamster immunoglobulin classes and subclasses by affinity chromatography on protein A and selective elution was studied using 0.1 M phosphate buffer, pH 8. The IgG fraction was completely absorbed, while IgM did not bind. Sequential application of buffers of decreasing pH allowed the elution of pure IgG2 (eluted at pH 6) and IgG1 (eluted at pH 5). Both subclasses were fully recovered. IgG2 could be subfractionated into 2 peaks eluted respectively at pH 6.5 and 6. Immunodiffusion of the whole IgG2 fraction against anti-hamster immunoglobulin serum gave 2 precipitation lines. One of these lines was missing in the pH 6.5 fraction. Until now only 2 IgG subclasses have been described and these results suggest heterogeneity of hamster IgG2.
利用蛋白A亲和层析和选择性洗脱法对仓鼠免疫球蛋白类别和亚类进行分离的研究中，使用pH值为8的0.1M磷酸盐缓冲液。IgG组分被完全吸附，而IgM不结合。依次应用pH值递减的缓冲液可洗脱纯化的IgG2（在pH 6时洗脱）和IgG1（在pH 5时洗脱）。两个亚类均得到完全回收。IgG2可进一步分离为分别在pH 6.5和pH 6时洗脱的两个峰。用抗仓鼠免疫球蛋白血清对整个IgG2组分进行免疫扩散，得到两条沉淀线。在pH 6.5的组分中缺少其中一条线。到目前为止，仅描述了2种IgG亚类，这些结果提示仓鼠IgG2存在异质性。
