Wu J J, Phan H, Lam K S
Selectide Corporation, A Subsidiary of Hoechst Marion Roussel, Inc., Tucson, AZ 85737, USA.
Bioorg Med Chem Lett. 1998 Sep 8;8(17):2279-84. doi: 10.1016/s0960-894x(98)00413-2.
We studied the intrinsic tyrosine kinase activity and substrate specificity of c-Abl and Bcr-Abl protein tyrosine kinases (PTKs) using the peptide substrates discovered from a synthetic combinatorial peptide library. Our data indicate that the phosphorylation of these peptides by Bcr-Abl was consistently stronger than that by c-Abl. Bcr-Abl also showed substrate preference towards those peptides with one or more positive charges.
我们使用从合成组合肽库中发现的肽底物，研究了c-Abl和Bcr-Abl蛋白酪氨酸激酶（PTK）的内在酪氨酸激酶活性和底物特异性。我们的数据表明，Bcr-Abl对这些肽的磷酸化作用始终强于c-Abl。Bcr-Abl对那些带有一个或多个正电荷的肽也表现出底物偏好性。
