Meyer H H, Jungblut P W
Hoppe Seylers Z Physiol Chem. 1983 Jun;364(6):757-68. doi: 10.1515/bchm2.1983.364.1.757.
The steroid-binding core of estradiol receptor was purified from pig uterus cytosol by a protocol consisting of (1) adsorption to heparin-sepharose, (2) enzymatic release of the receptor core, (3) DEAE-chromatography, (4) Sephadex G-150 filtration and (5) chromatography on heparin-sepharose. The final product was approximately 18000-fold enriched over the starting material. It consisted of at least 18% core protein resembling dimeric microsomal receptor with a molecular mass of 75 kDa and an isoelectric point of 5.8 (microheterogeneity). A goat antiserum raised against the preparation contains immunoglobulins G precipitating estradiol-receptor complexes, and antibodies releasing the steroid from its binding site.
（1）吸附到肝素 - 琼脂糖上；（2）酶促释放受体核心；（3）DEAE - 柱层析；（4）葡聚糖凝胶G - 150过滤；（5）肝素 - 琼脂糖层析。最终产物相对于起始材料富集了约18000倍。它至少由18%的核心蛋白组成，该核心蛋白类似于二聚体微粒体受体，分子量为75 kDa，等电点为5.8（微不均一性）。针对该制剂产生的山羊抗血清含有能沉淀雌二醇 - 受体复合物的免疫球蛋白G，以及能从其结合位点释放类固醇的抗体。
