Interactions between Mouse Immunoglobulins and Staphylococcal Protein A
Interactions between Mouse Immunoglobulins and Staphylococcal Protein A
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小鼠免疫球蛋白和葡萄球菌蛋白 A 之间的相互作用
DOI：
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发表时间：
1979
影响因子：
3.7
通讯作者：
J. Vaerman
中科院分区：
文献类型：
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作者：
M. Chalon;R. Milne;J. Vaerman
当将小鼠血清或腹水上样到蛋白A-琼脂糖凝胶柱上并用足够的磷酸盐缓冲盐水洗涤时，通常在未结合蛋白的第一个主峰之后用相同的缓冲液洗脱第二个蛋白峰。该第二个峰几乎是纯IgG 1。随后用酸性盐水洗脱更多的IgG I加上IgG 2a、IgG 2b和IgG 3，用中性缓冲液洗脱的90%的IgG 1可以用相同的缓冲液在相同的延迟位置重新洗脱。当在未结合蛋白质的主峰之后开始从0至3 M硫氰酸钠的梯度时，所有IgG I在IgG 2和IgG 3之前洗脱。这些结果表明，IgG 1对蛋白A的亲和力比IgG 2或IgG 3低得多，并且正常小鼠血清IgG 1可以通过这种简单的方法纯化。
When mouse serum or ascites is applied on protein A‐Sepharose columns and washed with enough phosphate‐buffered saline, a second protein peak is often eluted with the same buffer after the first major peak of unbound proteins. This second peak is almost pure IgG1. More IgG I plus IgG2a, IgG2b and IgG3 are thereafter eluted with acid saline, 90% of the IgG1 which had been eluted with neutral buffer could be re‐eluted at the same retarded position with the same buffer. When a gradient from 0 to 3 M sodium thiocyanate was started after the major peak of unbound proteins, all IgG I was eluted before IgG2 and IgG3. These results suggest that IgG1 has a much lower affiniiy for protein A than IgG2 or IgG3 and that normal mouse serum IgG1 can be purified by such a simple procedure.