Sato K, Miki S, Tachibana H, Hayashi F, Akiyama T, Fukami Y
Department of Biology, Faculty of Science, Kobe University, Japan.
Biochem Biophys Res Commun. 1990 Sep 28;171(3):1152-9. doi: 10.1016/0006-291x(90)90805-w.
A 21-residue synthetic peptide corresponding to a part of the noncatalytic domain of p60v-src (residues 137 to 157) was found to inhibit the tyrosine kinase activity of p60v-src. The half inhibition concentration was ca. 7.5 microM. The peptide (peptide A) did not compete with substrate proteins or ATP. Peptide A also inhibited the autophosphorylation of epidermal growth factor receptor/kinase and the tyrosine-specific protein phosphorylation in the acetylcholine receptor-rich membranes isolated from electroplax of Narke japonica. However, serine/threonine-specific protein kinases such as cAMP-dependent and cGMP-dependent protein kinases were not inhibited by peptide A.
发现一段与p60v-src非催化结构域一部分（第137至157位氨基酸残基）相对应的21个氨基酸残基的合成肽可抑制p60v-src的酪氨酸激酶活性。半数抑制浓度约为7.5微摩尔。该肽（肽A）不与底物蛋白或ATP竞争。肽A还抑制表皮生长因子受体/激酶的自磷酸化以及从日本电鳐电器官分离的富含乙酰胆碱受体的膜中的酪氨酸特异性蛋白磷酸化。然而，丝氨酸/苏氨酸特异性蛋白激酶，如cAMP依赖性和cGMP依赖性蛋白激酶，不受肽A抑制。
