Eleanor Erikson

TL;DR: Sera from rabbits bearing tumors induced by Rous sarcoma virus were previously found to contain antibody to the RSV transforming protein, pp60 src, but two additional transformation-specific phosphoproteins from RSV-transformed avian cells are immunoprecipitated with these sera.

TL;DR: The avian sarcoma virus (ASV) protein responsible for cellular transformation in vitro and sarcomagenesis in animals was studied structurally with special reference to the sites of phosphorylation on the polypeptide, finding that pp60src contained two major sites ofosphorylation, one involving phosphoserine and the other involving phosphothreonine and possible addtional minor sites.

TL;DR: The methionine-containing tryptic peptides from the polypeptides of Mr 60,000 obtained from translation in vitro and from immunoprecipitation were found to be identical upon two-dimensional fractionation.

TL;DR: The phosphotransferase activity of the Rous sarcoma virus src gene product, pp60src, was inhibited both in vitro and in vivo by the bioflavonoid quercetin and studies in vitro showed that this flavonoid did not inhibit the phosphorylation of physiological substrates of this enzyme.

TL;DR: This report extends the previous studies concerning the identification and characterization of a protein from normal cells that is closely related to the avian sarcoma virus (ASV) transforming gene product pp60src to have an associated protein kinase activity analogous to that previously described for the viral pp60 src.