RAPID, NOVEL METHOD FOR SOLID-PHASE DERIVATIZATION OF IGG ANTIBODIES FOR IMMUNE-AFFINITY CHROMATOGRAPHY
RAPID, NOVEL METHOD FOR SOLID-PHASE DERIVATIZATION OF IGG ANTIBODIES FOR IMMUNE-AFFINITY CHROMATOGRAPHY
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DOI：
10.1016/0022-1759(78)90133-3
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发表时间：
1978-01-01
影响因子：
2.2
通讯作者：
MARCHALONIS, JJ
中科院分区：
文献类型：
--
作者：
GERSTEN, DM;MARCHALONIS, JJ
用琼脂糖凝胶共价结合金黄色葡萄球菌A蛋白，从兔抗血清中分离免疫球蛋白G组分，制得固相免疫吸附剂。然后使用交联剂二甲基硫代亚胺将免疫球蛋白偶联到基质上。以这种方式结合的免疫球蛋白抗体与抗原[Ag]结合的方向是正确的，因为与蛋白A的结合是通过免疫球蛋白分子的Fc部分发生的，从而使分子的结合部位自由地与抗原相互作用。
A solid-phase immune adsorbent can be prepared from rabbit antiserum by isolating the Ig[immunoglobulin]G fraction with protein A of Staphylococcus aureus associated covalently with a Sepharose matrix. The IgG is then coupled to the matrix using the cross-linking agent dimethylsuberimidate. IgG antibody bound in this fashion is in the proper orientation for combination with antigen [Ag] because association with protein A occurs via the Fc portion of the IgG molecule, thus leaving the combining site of the molecule free to interact with Ag.