This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Brugge, J Articles by Erikson, R I Search for Related Content PubMed PubMed Citation Articles by Brugge, J Articles by Erikson, R I

 Previous Article  |  Next Article 

J Virol. 1978 June; 26(3): 773-782

Peptide analysis of the transformation-specific antigen from avian sarcoma virus-transformed cells.

ABSTRACT

Sera from rabbits bearing tumors induced by avian sarcoma virus (ASV) were ussed to immunopecipitate virus-specific proteins from extracts of chicken, hamster, and field vole cells transformed by ASV. Two virus-specific proteins having molecular weights of 76,000 and 60,000 were found in all cell lines examined. The 76,000-molecular-weight protein, Pr76, is the precursor to the internal core proteins of ASV. The 60,000-molecular-weight (60K) transformation-specific antigen from each cell line was subjected to peptide analysis, using chymotrypsin and Staphylococcus aureus V8 protease. The resulting peptide maps of the 60K protein from the different ASV-infected cell types were similar for each enzyme, strongly suggesting that the 60K protein is virus coded. Two-dimensional analysis of chymotryptic peptides from Pr76 and 60K reveals that 60K is not related to the gs antigen precursor. Radiolabeling of ASV-transformed cells with inorganic phosphate revealed that 60K is phosphorylated in vivo. The 60K proteins isolated from both ASV-transformed chicken and field vole cells were found to contain one tryptic phosphopeptide. The tryptic phosphopeptides of 60K from both cell lines migrated identically upon two-dimensional peptide analyses, and their migration differed from that of the principal phosphopeptide of Pr76.