Work

Purification of simian virus 40 large T antigen by immunoaffinity chromatography

Year: 1985

Type: article

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.

Source: Journal of Virology

DOI: 10.1128/jvi.53.3.1001-1004.1985

Authors: R A Dixon, D Nathans

Language: English

Topic: Polyomavirus and related diseases

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

Open Access status: bronze

Funder: National Cancer Institute

Awards: Program on Molecular and Cellular Mechanisms of Tumorigenesis, G970855588

OpenAlex ID: W1934622753