De Sombre E R, Puca G A, Jensen E V
Proc Natl Acad Sci U S A. 1969 Sep;64(1):148-54. doi: 10.1073/pnas.64.1.148.
A method has been devised for purifying the estrogen-binding protein ("uptake receptor") of uterine cytosol which circumvents the marked tendency of this receptor to aggregate during attempted isolation. Ammonium sulfate precipitation of the estradiol-receptor complex of calf uterine cytosol in the presence of calcium ions yields both an 8S complex and its 4S subunit which are stable during further purification by gel filtration and ion exchange chromatography. The major product is the 4S complex which does not revert to 8S in the absence of salt and which has been purified about 2500-fold. The approximate isoelectric points of these partially purified 8S and 4S complexes are 5.8 and 6.4, respectively.
已经设计出一种用于纯化子宫胞质溶胶中雌激素结合蛋白（“摄取受体”）的方法，该方法避免了这种受体在尝试分离过程中明显的聚集倾向。在钙离子存在下，对小牛子宫胞质溶胶的雌二醇受体复合物进行硫酸铵沉淀，可产生一种8S复合物及其4S亚基，它们在通过凝胶过滤和离子交换色谱进一步纯化的过程中是稳定的。主要产物是4S复合物，它在无盐情况下不会恢复为8S，并且已纯化约2500倍。这些部分纯化的8S和4S复合物的近似等电点分别为5.8和6.4。
