Sjödin L, Holmberg K, Lyden A
Endocrinology. 1984 Sep;115(3):1102-9. doi: 10.1210/endo-115-3-1102.
The characteristics of interaction of insulin with specific receptors on exocrine pancreatic cells of the guinea pig have been studied. Insulins from different species as well as certain insulin analogs were found to have affinities to receptors on pancreatic acinar cells which are similar to what have been described for insulin receptors in other organs of different mammalian species. Binding was rapid and reversible at 37 C but dissociation was markedly slower at 12 C. Clear indications of negative cooperativity between binding sites were not seen. Bovine and chicken insulin bound with approximately a 100-fold higher affinity to guinea pig insulin receptors than guinea pig insulin itself. The number of insulin receptors per acinar cell were comparable with what has been described for other mammalian cells. Part of cell-associated insulin was internalized. After 60 min of incubation the major part of radioactivity in the incubation medium as well as in cells appeared as intact [125I] iodoinsulin on a Sephadex G-50 column and less than 12% of radioactivity was eluted as breakdown products together with Na 125I.
对豚鼠胰腺外分泌细胞上胰岛素与特定受体的相互作用特性进行了研究。发现来自不同物种的胰岛素以及某些胰岛素类似物对胰腺腺泡细胞上的受体具有亲和力，这与在不同哺乳动物物种的其他器官中所描述的胰岛素受体情况相似。在37℃时结合迅速且可逆，但在12℃时解离明显较慢。未观察到结合位点之间负协同作用的明确迹象。牛胰岛素和鸡胰岛素与豚鼠胰岛素受体的结合亲和力比豚鼠胰岛素本身高约100倍。每个腺泡细胞上胰岛素受体的数量与其他哺乳动物细胞中所描述的相当。部分与细胞结合的胰岛素被内化。孵育60分钟后，孵育培养基以及细胞中大部分放射性在Sephadex G - 50柱上以完整的[125I]碘胰岛素形式出现，并且不到12%的放射性与碘化钠一起作为降解产物被洗脱。
