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Purification of simian virus 40 large T antigen by immunoaffinity chromatography. |
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| Authors: | R A Dixon and D Nathans |
| 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. |
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