Inaba M, Katayama S, Akabane S, Maruno Y, Itabashi A, Ishii J
Fourth Department of Medicine, Saitama Medical School.
Nihon Naibunpi Gakkai Zasshi. 1993 Jun 20;69(6):632-5. doi: 10.1507/endocrine1927.69.6_632.
With iodinated vasopressin analogue, d(CH2)5[Tyr(Me)2, Tyr(NH2)9] AVP, at position 9, followed by purification by HPLC (specific activity 473-543Ci/mmol), a specific binding was observed in the rat liver plasma membrane fraction. Scatchard analysis indicated a single class of high-affinity binding sites with a Kd of 0.23nM and Bmax of 142fmol/mg protein. V2-agonist, DDAVP, did not displace 125I-vasopressin analogue. These results suggest that 125I-d(CH2)5[Tyr(Me)2, Tyr(NH2)9] AVP with a high specific activity is a useful tool to investigate V1-receptors.
使用碘化血管加压素类似物d(CH2)5[Tyr(Me)2, Tyr(NH2)9]AVP（在第9位），随后通过高效液相色谱法进行纯化（比活性为473 - 543Ci/mmol），在大鼠肝细胞膜组分中观察到特异性结合。Scatchard分析表明存在一类单一的高亲和力结合位点，解离常数（Kd）为0.23nM，最大结合容量（Bmax）为142fmol/mg蛋白质。V2激动剂去氨加压素（DDAVP）不能取代125I - 血管加压素类似物。这些结果表明，具有高比活性的125I - d(CH2)5[Tyr(Me)2, Tyr(NH2)9]AVP是研究V1受体的有用工具。
