title: Purification of simian virus 40 large T antigen by immunoaffinity chromatography.
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.
authors.forename: R A
authors.initials: RA
authors.lastname: Dixon
authors.forename: D
authors.initials: D
authors.lastname: Nathans
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor / Q000276:immunology / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D000882:Haplorhini; D013539:Simian virus 40 / Q000276:immunology*; D014764:Viral Proteins / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D000911:Antibodies, Monoclonal; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor; D014764:Viral Proteins