Mahrenholz A M, Votaw P, Roach P J, Depaoli-Roach A A, Zioncheck T F, Harrison M L, Geahlen R L
Department of Biochemistry, Indiana University School of Medicine, Indianapolis 46223.
Biochem Biophys Res Commun. 1988 Aug 30;155(1):52-8. doi: 10.1016/s0006-291x(88)81048-9.
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.
从兔骨骼肌中分离得到的糖原合酶，可被一种从牛胸腺中纯化出的蛋白酪氨酸激酶p40磷酸化。磷酸化的化学计量比为0.4 - 0.5摩尔/摩尔亚基，且针对EEDGERYDEDEE序列中的单个酪氨酸残基具有特异性。这个酸性序列与红细胞带3蛋白中被p40识别的位点有相当大的相似性。在对磷酸化肽段的分析中，发现序列-RY(P)-会阻碍胰蛋白酶或自动Edman降解的切割作用。
