Characterization of the amino terminal tryptic peptide of simian virus 40 small-t and large-T antigens

A. Mellor, A. E. Smith

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Simian virus 40 small-t and large-T antigen were synthesized in vitro and labeled with methionine donated by initiator tRNA. Tryptic peptide fingerprinting was used to identify the amino-terminal peptide of the two proteins. Similar fingerprint analysis of small-t and large-T made in vitro in the absence of acetyl coenzyme A showed that the mobility of the amino-terminal peptide was changed under these conditions and suggested that it is acetylated. These data establish that the amino-terminal methionine residue of simian virus 40 small-t and large-T results from an initiation event, not post-translational cleavage, and provides additional evidence that the amino terminus of both proteins is acetylated. The identification of the amino-terminal peptide provides a useful marker for further studies on different forms of T-antigen from cells infected with and transformed by simian virus 40 and related viruses.

Original languageEnglish (US)
Pages (from-to)992-996
Number of pages5
JournalJournal of Virology
Volume28
Issue number3
StatePublished - Dec 1 1978

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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