二硫键还原将人胎盘胰岛素受体转变为低亲和力形式。
Disulfide reduction converts the insulin receptor of human placenta to a low affinity form.
作者信息
Jacobs S, Cuatrecasas P
出版信息
J Clin Invest. 1980 Dec;66(6):1424-7. doi: 10.1172/JCI109996.
Abstract
Treatment of human placenta membranes with dithiothrietol (DTT) followed by N-ethylmaleimide results in a 60% reduction in insulin binding. Treatment with N-ethylmaleimide alone has little effect. The decrease in insulin binding that results from DTT treatment is due to a decrease in affinity for insulin, with little change in total receptor number. DTT has similar effects on receptor solubilized from placenta membranes with Triton X-100, indicating that its effects are not attributable to changes in the arrangement of receptors in the membrane. In contrast to placenta membranes, treatment of liver membranes with DTT does not decrease insulin binding. These results suggest that reduction of a critical disulfide bond in insulin receptors from human placenta converts the receptor to a low affinity form.
摘要
用二硫苏糖醇（DTT）处理人胎盘膜，随后用N-乙基马来酰亚胺处理，可使胰岛素结合减少60%。单独用N-乙基马来酰亚胺处理几乎没有效果。DTT处理导致的胰岛素结合减少是由于对胰岛素的亲和力降低，而总受体数量变化不大。DTT对用Triton X-100从胎盘膜中溶解的受体有类似作用，表明其作用并非归因于膜中受体排列的变化。与胎盘膜相反，用DTT处理肝膜不会降低胰岛素结合。这些结果表明，人胎盘胰岛素受体中一个关键二硫键的还原将受体转化为低亲和力形式。
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引用本文的文献
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本文引用的文献
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The subunit structure of rat liver insulin receptor. Antibodies directed against the insulin-binding subunit.大鼠肝脏胰岛素受体的亚基结构。针对胰岛素结合亚基的抗体。
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Affinity chromatography of insulin receptors.胰岛素受体的亲和层析
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