The EGF receptor-kinase has multiple phosphorylation sites.
The EGF receptor-kinase has multiple phosphorylation sites.
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EGF 受体激酶具有多个磷酸化位点。
DOI：
10.1016/s0006-291x(82)80010-7
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发表时间：
1982
影响因子：
3.1
通讯作者：
KingJr,LE
中科院分区：
文献类型：
--
作者：
Gates,RE;KingJr,LE
15 μM [γ-~（32）P] ATP标记的表皮生长因子（EGF）受体-激酶在十二烷基硫酸钠聚丙烯酰胺凝胶电泳中的表观分子量，当标记过程中有EGF存在时，增加达10 K道尔顿。在非常低的ATP浓度下磷酸化的EGF受体激酶可以通过在存在和不存在添加EGF的情况下添加过量的未标记的ATP而转移到更高的分子量。胰蛋白酶肽图从EGF受体激酶磷酸化在低和高ATP浓度显示四个主要的磷酸化肽。4个主要的磷酸化胰蛋白酶肽的存在和磷酸盐掺入量的分子量变化的依赖性表明，多个磷酸化位点上存在的受体激酶。
The apparent molecular weight in sodium dodecyl sulfate polyacrylamide gel electrophoresis of epidermal growth factor (EGF) receptor-kinase labeled with 15 μM [γ-32P] ATP increased as much as 10K daltons when EGF was present during labeling. The EGF receptor-kinase phosphorylated at very low ATP concentrations could be shifted to higher molecular weight by adding excess unlabeled ATP both in the presence and absence of added EGF. Tryptic peptide maps made from the EGF receptor-kinase phosphorylated at low and high ATP concentrations showed four major phosphorylated peptides. The presence of 4 major phosphorylated tryptic peptides and the dependency of the molecular weight shift on the amount of phosphate incorporated suggested that multiple phosphorylation sites are present on the receptor-kinase.