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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izdano v:	J Virol
Principais autores:	Dixon, R A, Nathans, D
Format:	Artigo
Jezik:	Inglês
Izdano:	American Society for Microbiology (ASM) 1985
Teme:	Research Article
Online dostop:	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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