Phosphorylation of protein tyrosine by human erythrocyte casein kinase A.
Phosphorylation of protein tyrosine by human erythrocyte casein kinase A.
复制标题
人红细胞酪蛋白激酶 A 对蛋白酪氨酸的磷酸化。
DOI：
10.1016/s0006-291x(86)80256-x
复制
发表时间：
1986
影响因子：
3.1
通讯作者：
Tao,M
中科院分区：
文献类型：
--
作者：
Lu,PW;Tao,M
人红细胞酪蛋白激酶A，以前被鉴定为丝氨酰、苏氨酰激酶，也被发现催化蛋白酪氨酸的磷酸化。在血管紧张素-II和几种含酪氨酸的合成肽中检测到酪氨酸残基的磷酸化。此外，在烷基化牛血清白蛋白和从人红细胞膜纯化的带3和锚蛋白中也观察到酪氨酰残基的磷酸化。磷酸酪氨酸的鉴定进行了使用二维薄层电泳在pH 1.9和3.5后，酸水解的磷蛋白。然而，应该指出的是，在带3和锚蛋白催化酪蛋白激酶A的主要磷酸化位点是丝氨酰和苏氨酰残基。
Human erythrocyte casein kinase A, previously identified as a seryl, threonyl kinase, was found also to catalyze the phosphorylation of protein tyrosine. Phosphorylation of tyrosyl residues was detected in angiotensin-II and in several tyrosine containing synthetic peptides. In addition, phosphorylation on tyrosyl residues was also observed in alkylated bovine serum albumin and in band 3 and ankyrin purified from human erythrocyte membranes. The identification of phosphotyrosine was conducted using two-dimensional thin layer electrophoresis at pH 1.9 and 3.5 after acid hydrolysis of the phosphoproteins. It should be noted, however, that the major phosphorylation sites in band 3 and ankyrin catalyzed by casein kinase A were seryl and threonyl residues.