Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40.
Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40.
复制标题
牛胸腺蛋白酪氨酸激酶 p40 对糖原合酶的磷酸化。
DOI：
10.1016/s0006-291x(88)81048-9
复制
发表时间：
1988
影响因子：
3.1
通讯作者：
Geahlen,RL
中科院分区：
文献类型：
--
作者：
Mahrenholz,AM;Votaw,P;Roach,PJ;Depaoli-Roach,AA;Zioncheck,TF;Harrison,ML;Geahlen,RL
兔骨骼肌糖原合酶被从牛胸腺中纯化的蛋白酪氨酸激酶p40磷酸化。磷酸化的化学计量为0.4-0.5 mol/mol亚基，对序列EEDGERYDEDEE中的单个酪氨酸残基具有特异性。该酸性序列与红细胞带3蛋白中p40识别的位点具有相当大的相似性。在磷酸化肽的分析中，注意到序列-RY（P）-阻碍胰蛋白酶或自动Edman降解的切割。
Glycogen synthase from rabbit skeletal muscle was found to be phosphorylated by a protein-tyrosine kinase, p40, purified from bovine thymus. The phosphorylation, to a stoichiometry of 0.4–0.5 mol/mol subunit, was specific for a single tyrosine residue in the sequence EEDGERYDEDEE. This acidic sequence has considerable similarity to the site recognized by p40 in erythrocyte band 3 protein. In the analysis of the phosphorylated peptide, it was noted that the sequence —RY (P)— impeded cleavage by either trypsin or automatic Edman degradation.