| Literature DB >> 2983081 |
Abstract
Simian virus 40 large T antigen from lytically infected cells has been purified to near homogeneity by immunochromatography of the cell extract on a protein A-Sepharose-monoclonal antibody column. The resulting T antigen retains biochemical activity; i.e., it hydrolyzes ATP and binds to simian virus 40 DNA at the origin of replication.Entities:
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Year: 1985 PMID: 2983081 PMCID: PMC254743
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103