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

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...

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Bibliographic Details
Published in:J Virol
Main Authors: Dixon, R A, Nathans, D
Format: Artigo
Language:Inglês
Published: American Society for Microbiology (ASM) 1985
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Research Article
Online Access:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC254743/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2983081/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.53.3.1001-1004.1985
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