Yu K T, Gould M K
Am J Physiol. 1978 Dec;235(6):E606-13. doi: 10.1152/ajpendo.1978.235.6.E606.
The specific binding of 125I-insulin by rat soleus muscle was depressed when muscle ATP was depleted, either by prolonged anoxia or more rapidly with 2,4-dinitrophenol. Insulin binding was not eliminated in ATP-depleted muscle, but was reduced by 70--80%. Insulin binding by aerobic muscle could be resolved into two components; a high-affinity, low-capacity site (KD = 7.8 nM) and a low-affinity, high-capacity site (KD = 390 nM). The stimulatory effect of insulin on xylose uptake could be correlated with binding to the high-affinity site. These results indicate that there is some ATP-dependent process involved in the regulation of insulin binding by soleus muscle. It is suggested that this could be a phosphorylation-dephosphorylation system, acting either on the receptor itself or on some closely related membrane protein.
当大鼠比目鱼肌的三磷酸腺苷（ATP）耗尽时，无论是通过长时间缺氧还是用2,4-二硝基苯酚更快地耗尽，125I-胰岛素与之的特异性结合都会受到抑制。在ATP耗尽的肌肉中，胰岛素结合并未消除，但减少了70%至80%。有氧肌肉中的胰岛素结合可分为两个成分：一个高亲和力、低容量位点（解离常数KD = 7.8纳摩尔）和一个低亲和力、高容量位点（KD = 390纳摩尔）。胰岛素对木糖摄取的刺激作用可能与和高亲和力位点的结合有关。这些结果表明，比目鱼肌中存在一些依赖ATP的过程参与胰岛素结合的调节。有人提出，这可能是一个磷酸化-去磷酸化系统，作用于受体本身或一些密切相关的膜蛋白。
