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. 1978 Dec;28(3):992–996. doi: 10.1128/jvi.28.3.992-996.1978

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

A Mellor, A E Smith
PMCID: PMC525822  PMID: 215789

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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