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...
Uloženo v:
| Vydáno v: | J Virol |
|---|---|
| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1985
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| Témata: | |
| On-line přístup: | 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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