Abstract
All the known avian sarcoma viruses have associated protein kinase activities that phosphorylate tyrosine residues of their target proteins. A decapeptide fragment of pp60src of Rous sarcoma virus (RSV), residues 415-424, and an analog of that sequence have been chemically synthesized by solid-phase methods. The two decapeptides were not phosphorylated by pp60src of RSV, P90 of Y73 avian sarcoma virus, or P140 of Fujinami sarcoma virus. However, both peptides were able to inhibit competitively the kinase activities associated with the transforming proteins. Antiserum was raised against one of the peptides and IgG was purified from the serum by affinity chromatography. The antibody was able to precipitate pp60src of RSV as well as P90 of Y73 virus from cells infected with these viruses. The antibody also precipitated a number of high molecular weight phosphoproteins from normal chicken and rat fibroblasts and from several lines of virus-transformed cells.
MeSH Terms
Animals
Cells, Cultured
Chick Embryo
Cross Reactions
Oncogene Protein pp60(v-src)
Peptide Fragments/chemical synthesis,immunology,pharmacology
Phosphoproteins/immunology
Protein Kinase Inhibitors
Protein Kinases/immunology
Rats
Viral Proteins/immunology
Chemicals
Peptide Fragments
Phosphoproteins
Protein Kinase Inhibitors
Viral Proteins
Protein Kinases
Oncogene Protein pp60(v-src)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wong T W
Goldberg A R
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