Raam S, Vrabel D M
Tufts University School of Medicine, Tufts University Medical Cancer Unit at Lemuel Shattuck Hospital, Boston, MA 02130.
Clin Chem. 1988 Oct;34(10):2053-7.
We present evidence to show that monoclonal antibodies to estrogen receptors (ER) in solid phase recognize the secondary estrogen binding sites with moderate to low affinity for estradiol (E2). An excellent quantitative agreement was found in five cytosols between the ER values obtained by the enzyme immunoassay (ER-EIA) and the amount of secondary estrogen binding sites measured by the assay involving dextran-coated charcoal (Clin Chem 1986;32:1496). The immunoreactive protein recognized by the antibody-coated beads, when allowed to react with ER(+) cytosols, is shown to bind [3H]estradiol only when the ligand concentration exceeds 8 nmol/L. Further biochemical and functional characterization of the immunoreactive protein is required to establish similarities/dissimilarities between this protein, high-affinity Type I ER sites, and the secondary sites such as Type II sites.
我们提供的证据表明，固相抗雌激素受体（ER）单克隆抗体以中等到低的亲和力识别雌二醇（E2）的二级雌激素结合位点。通过酶免疫测定（ER-EIA）获得的ER值与通过葡聚糖包被活性炭测定法测量的二级雌激素结合位点数量之间，在五种细胞溶质中发现了极好的定量一致性（《临床化学》1986年；32:1496）。当抗体包被的磁珠识别的免疫反应性蛋白与ER(+)细胞溶质反应时，只有当配体浓度超过8 nmol/L时，才会显示出与[3H]雌二醇结合。需要对该免疫反应性蛋白进行进一步的生化和功能表征，以确定该蛋白、高亲和力I型ER位点以及II型位点等二级位点之间的异同。
