Jungblut P W, Hekim N, Meyer H H, Szendro P I
J Steroid Biochem. 1983 Jul;19(1A):87-94.
A goat antiserum was raised by immunization with the endoglycosidase fission product of porcine estrogen receptor. Its IgG fraction was employed for ascertaining the interrelationship of receptor forms extracted from three subcellular compartments of target cells and for comparing receptors from various species. Unspecific alignments of (non-immune) IgGs giving rise to soluble complexes were avoided by removal of the receptor entity responsible with carrier-attached trypsin. Coincubation of the estradiol-tagged tryptic receptor cores and immune IgG resulted in the formation of labelled precipitates and in the release of estradiol from its binding site, in every instance tested. A minimum of three common antigenic determinants must therefore exist not only on all porcine receptor forms, but also on human, ovine, bovine, rabbit, guinea-pig and rat estrogen receptors, pointing to a high degree of phylogenetic conservation.
用猪雌激素受体的内切糖苷酶裂解产物免疫制备了山羊抗血清。其IgG组分用于确定从靶细胞的三个亚细胞区室提取的受体形式之间的相互关系，以及比较不同物种的受体。通过用载体连接的胰蛋白酶去除负责的受体实体，避免了（非免疫）IgG产生可溶性复合物的非特异性结合。在每个测试实例中，雌二醇标记的胰蛋白酶受体核心与免疫IgG共同孵育导致形成标记沉淀，并使雌二醇从其结合位点释放。因此，至少三个共同的抗原决定簇不仅必须存在于所有猪受体形式上，而且也存在于人类、绵羊、牛、兔、豚鼠和大鼠的雌激素受体上，这表明了高度的系统发育保守性。
