[HTML][HTML] c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct …
BB Brasher, RA Van Etten - Journal of Biological Chemistry, 2000 - ASBMB
Using the specific Abl tyrosine kinase inhibitor STI 571, we purified unphosphorylated
murine type IV c-Abl and measured the kinetic parameters of c-Abl tyrosine kinase activity in
a solution with a peptide-based assay. Unphosphorylated c-Abl exhibited substantial
peptide kinase activity with K m of 204 μm and V max of 33 pmol min− 1. Contrary to
previous observations using immune complex kinase assays, we found that a transforming c-
Abl mutant with a Src homology 3 domain point mutation (P131L) had significantly (about 6 …
murine type IV c-Abl and measured the kinetic parameters of c-Abl tyrosine kinase activity in
a solution with a peptide-based assay. Unphosphorylated c-Abl exhibited substantial
peptide kinase activity with K m of 204 μm and V max of 33 pmol min− 1. Contrary to
previous observations using immune complex kinase assays, we found that a transforming c-
Abl mutant with a Src homology 3 domain point mutation (P131L) had significantly (about 6 …