Poirier J C, Combarnous Y, Blanc M R
Acta Endocrinol (Copenh). 1984 May;106(1):38-42. doi: 10.1530/acta.0.1060038.
Antibodies recognizing determinants of the alpha-subunit, which is common to all glycoprotein hormones, were eliminated from antisera against native oFSH by affinity chromatography. Since the free alpha-subunit is immunologically different from the alpha-subunit in the intact hormone, we did not use an alpha-subunit affinity column. Instead, the antisera were applied to an LH affinity column. However, because intact LH dissociates in the conditions used to elute the purified antibodies, we prepared an LH derivative with covalently-linked subunits and coupled it to gel matrix. By this method oFSH antisera were freed from their non-specific antibodies. The cross-reaction of ovine lutropin in the oFSH radioimmunoassay (RIA) was lowered from 2% to less than 0.1%. Moreover, as the columns can be used repeatedly over long periods with no apparent loss of efficiency, large volumes of antiserum can be treated in this manner.
通过亲和层析法，从针对天然羊促卵泡素（oFSH）的抗血清中去除了识别α亚基决定簇的抗体，α亚基是所有糖蛋白激素所共有的。由于游离的α亚基在免疫上与完整激素中的α亚基不同，所以我们没有使用α亚基亲和柱。相反，将抗血清应用于促黄体生成素（LH）亲和柱。然而，由于完整的LH在用于洗脱纯化抗体的条件下会解离，我们制备了一种亚基共价连接的LH衍生物，并将其偶联到凝胶基质上。通过这种方法，oFSH抗血清中的非特异性抗体被去除。在oFSH放射免疫分析（RIA）中，羊促黄体素的交叉反应率从2%降至低于0.1%。此外，由于这些柱子可以长时间重复使用而效率无明显损失，因此可以用这种方式处理大量抗血清。
