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...
Сохранить в:
| Опубликовано в:: | J Virol |
|---|---|
| Главные авторы: | , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Microbiology (ASM)
1985
|
| Предметы: | |
| Online-ссылка: | 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 |
| Метки: |
Нет меток, Требуется 1-ая метка записи!
|