Abstract
It has recently been reported that the sequences of the sis oncogene of simian sarcoma virus (SSV) and of human platelet-derived growth factor (PDGF) are very similar1,2, establishing the most solid link yet between the mitogenic actions of growth factors and the transforming proteins of retroviruses. To investigate molecular mechanisms of transformation I have produced antisera against synthetic peptides corresponding to segments of the protein sequences predicted by the nucleotide sequences of viral oncogenes. Applying this approach to the case of sis and PDGF, I report here the results of probing outdated human platelets with an antiserum directed against a synthetic peptide representing residues 139–155 of the predicted sequence of the SSV transforming protein, p28sis (ref. 3). I detected peptides of apparent molecular weights (MWs) 30,000 to 31,000 (30–31K) and 16–18K, which correspond to the apparent molecular weights of nonreduced and reduced PDGF4–8. In addition, a peptide of MW 21,000 was detected in platelets and a protein of MW 56,000 was detected in SSV-infected marmoset cells.