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表皮生长因子受体上新的自磷酸化位点(P4)的鉴定。

Identification of a novel autophosphorylation site (P4) on the epidermal growth factor receptor.

作者信息

Hsuan J J, Totty N, Waterfield M D

机构信息

Structural Biology Group, Ludwig Institute for Cancer Research, London, U.K.

出版信息

Biochem J. 1989 Sep 1;262(2):659-63. doi: 10.1042/bj2620659.

Abstract

Three major autophosphorylation sites are located near the C-terminus of the epidermal growth factor receptor, but a fourth site is repeatedly detected. We report here the purification and sequencing of a tryptic peptide containing this site, Tyr-1086. Furthermore, we demonstrate that additional phosphopeptides are observed following both partial digestion and overdigestion. Finally, we show that Tyr-1086 can be phosphorylated in intact cells.

摘要

三个主要的自磷酸化位点位于表皮生长因子受体的C末端附近,但反复检测到第四个位点。我们在此报告了含有该位点(酪氨酸-1086)的胰蛋白酶肽段的纯化和测序。此外,我们证明在部分消化和过度消化后均观察到额外的磷酸肽段。最后,我们表明酪氨酸-1086在完整细胞中可以被磷酸化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a961/1133318/bcc6506d35ca/biochemj00200-0269-a.jpg

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