Korc M, Matrisian L M, Planck S R, Magun B E
Biochem Biophys Res Commun. 1983 Mar 29;111(3):1066-73. doi: 10.1016/0006-291x(83)91408-0.
Specific, saturable EGF receptors were demonstrated in isolated rat pancreatic acini. Binding of EGF to these receptors was one-half maximal at 20 min and maximal at 120 min. Scatchard analyses revealed a single order of binding sites with a Kd of 4.90 nM. Following binding, EGF was rapidly internalized and converted to two acidic species. EGF did not alter either basal amylase release or the rate of [3H]phenylalanine incorporation into TCA-precipitable protein. The finding of high affinity EGF receptors in pancreatic acinar cells supports the hypothesis that EGF participates in the long-term regulation of pancreatic exocrine function.
在分离的大鼠胰腺腺泡中证实了特异性、可饱和的表皮生长因子（EGF）受体。EGF与这些受体的结合在20分钟时达到最大结合量的一半，在120分钟时达到最大值。Scatchard分析显示存在单一顺序的结合位点，解离常数（Kd）为4.90 nM。结合后，EGF迅速内化并转化为两种酸性物质。EGF既不改变基础淀粉酶的释放，也不改变[3H]苯丙氨酸掺入三氯乙酸沉淀蛋白的速率。胰腺腺泡细胞中存在高亲和力EGF受体这一发现支持了EGF参与胰腺外分泌功能长期调节的假说。
