Mukku V R, Stancel G M
Endocrinology. 1985 Jul;117(1):149-54. doi: 10.1210/endo-117-1-149.
Uterine membranes contain high affinity [dissociation constant (Kd) = 0.36 nM], saturable binding sites for [125I]iodo-epidermal growth factor (EGF). The binding of [125I] iodo-EGF is specific since it is abolished by excess unlabeled EGF but not by excess unlabeled insulin, fibroblast growth factor, or multiplication-stimulating activity. Incubation of [125I] iodo-EGF with uterine membranes, followed by chemical cross-linking with disuccinimidyl suberate and detergent extraction reveals a major species of specifically bound EGF (mol wt = 170,000) and a minor species (mol wt = 150,000) visualized by autoradiography of sodium dodecyl sulfate gels after electrophoresis of the extracts. In detergent-solubilized preparations EGF also stimulates the phosphorylation of major (mol wt = 170,000) and minor (mol wt = 150,000) species of identical molecular weight. The increased phosphorylation produced by incubation of membrane extracts with EGF occurs largely at tyrosine residues, as indicated by phosphoamino acid analysis. These results indicate that the rat uterus contains high affinity EGF binding sites with the properties expected of EGF receptors.
子宫内膜含有高亲和力[解离常数（Kd）= 0.36 nM]的[125I]碘 - 表皮生长因子（EGF）饱和结合位点。[125I]碘 - EGF的结合具有特异性，因为过量未标记的EGF可消除该结合，但过量未标记的胰岛素、成纤维细胞生长因子或增殖刺激活性则不能。将[125I]碘 - EGF与子宫内膜一起孵育，随后用辛二酸二琥珀酰亚胺酯进行化学交联并进行去污剂提取，通过对提取物进行电泳后，对十二烷基硫酸钠凝胶进行放射自显影，可显示出一种主要的特异性结合EGF种类（分子量 = 170,000）和一种次要种类（分子量 = 150,000）。在去污剂溶解的制剂中，EGF还可刺激相同分子量的主要种类（分子量 = 170,000）和次要种类（分子量 = 150,000）的磷酸化。如磷酸氨基酸分析所示，膜提取物与EGF孵育所产生的磷酸化增加主要发生在酪氨酸残基上。这些结果表明，大鼠子宫含有具有EGF受体预期特性的高亲和力EGF结合位点。
