Yanaihara N, Yanaihara C, Iguchi K, Inoue T, Toyoshige M, Mochizuki T, Hoshino M, Kurokawa N, Kaneko T
University of Shizuoka School of Pharmaceutical Sciences, Japan.
Diabetes Res Clin Pract. 1989;7 Suppl 1:S109-13. doi: 10.1016/0168-8227(89)90096-x.
A peptide corresponding to the 957-980 sequence of human placental insulin receptor precursor (HIRP) was synthesized and antisera were produced against the synthetic peptide. Anti-synthetic HIRP(957-980) serum HIR-27 was proved to cross-react with HIRP-related proteins in solubilized human placental membranes. A radioimmunoassay developed with the antiserum and synthetic peptide HIRP(957-980) enabled us to separate, in combination with gel filtration, two insulin-binding components in solubilized human placental membranes which conceivably correspond to the alpha 2 beta 2 and alpha beta structures of the placental insulin receptor. The two components were shown to be distinct in insulin-binding behavior depending on conditions of pH and ionic strength in the binding assay.
合成了一段与人类胎盘胰岛素受体前体(HIRP)957 - 980序列相对应的肽,并针对该合成肽制备了抗血清。抗合成HIRP(957 - 980)血清HIR - 27被证明能与溶解的人胎盘膜中的HIRP相关蛋白发生交叉反应。用该抗血清和合成肽HIRP(957 - 980)开发的放射免疫测定法,使我们能够结合凝胶过滤,分离出溶解的人胎盘膜中的两种胰岛素结合成分,这两种成分可能分别对应胎盘胰岛素受体的α2β2和αβ结构。结果表明,在结合测定中,根据pH和离子强度条件,这两种成分在胰岛素结合行为上是不同的。