Isolation of proteins with kinase activity and related to pp60 src from human cells
Pavloff, N.; Biquard, J.M.; Hanania, N.; Semmel, M.
Biochemical and Biophysical Research Communications 121(3): 779-787
1984
ISSN/ISBN: 0006-291X PMID: 6204646 Document Number: 227174
A protein kinase activity (PK) was associated with immunoprecipitates between polypeptides of human lymphoblastoid cells of malignant origin (Raji cell line) or of their normal counterparts (Priess cell line) and antibodies directed against avian pp60-src or against the carboxyterminal hexapeptide of pp60-src. Thus, these human cells and Rous sarcoma virus transformed avian cells share antigenic determinants of pp60-src and, in particular, its carboxyterminal sequence, as well as one of its functions, a protein kinase activity. The protein kinase from Raji cells phosphorylated predominantly tyrosine residues, that from Priess cells threonine residues.