Harding J W, Erickson J B, Camara C C, Abhold R H, Wright J W
Neurosci Lett. 1986 Mar 28;65(1):23-8. doi: 10.1016/0304-3940(86)90114-x.
The combined hypothalamus-thalamus-septum and anteroventral third ventricular region (HTSA) of the rat was examined for [125I]angiotensin II ([125I]AII) binding using two protocols: one that preserved synaptosomal structure and a second that did not. Although maximum binding (Bmax) and dissociation constants (Kd) were similar in both preparations, high-performance liquid chromatographic analyses revealed that [125I]AII made up the majority of specifically bound label in the synaptosome preserved preparation while [125I]tyrosine ([125I]Tyr) represented most of the specifically bound label in the disrupted preparation. These results indicate that [125I]Tyr accumulation occurred subsequent to binding and degradation of [125I]AII and are consistent with the notion that rapid internalization of the receptor-[125I]AII complex occurs in those preparations where the synaptosomal structure remains intact.
利用两种方案对大鼠的下丘脑 - 丘脑 - 隔区及第三脑室前腹侧区域（HTSA）进行了[125I]血管紧张素II（[125I]AII）结合检测：一种方案可保留突触体结构，另一种则不能。尽管两种制剂中的最大结合量（Bmax）和解离常数（Kd）相似，但高效液相色谱分析显示，在保留突触体的制剂中，[125I]AII构成了特异性结合标记的大部分，而在破坏的制剂中，[125I]酪氨酸（[125I]Tyr）代表了大部分特异性结合标记。这些结果表明，[125I]Tyr的积累发生在[125I]AII结合和降解之后，并且与受体 - [125I]AII复合物在突触体结构保持完整的制剂中快速内化的观点一致。
