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Purification of simian virus 40 large T antigen by immunoaffinity chromatography.

By R A Dixon and D Nathans

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

Topics: Research Article
Year: 1985
OAI identifier: oai:pubmedcentral.nih.gov:254743
Provided by: PubMed Central
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