Purification of SV40 T-antigen by SV40 DNA-sepharose affinity chromatography
| Autor: | T. Hopkins-Davis, C. Payne, Barry I. Milavetz |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Adenosine Triphosphatases
Chromatography viruses Biophysics Simian virus 40 Cell Biology Hydroxylapatite Biochemistry Chromatography Affinity DNA-Binding Proteins Sepharose chemistry.chemical_compound Affinity chromatography chemistry Covalent bond DNA Viral Cyanogen bromide BamHI Antigens Viral Tumor Molecular Biology Polyacrylamide gel electrophoresis DNA |
| Zdroj: | Biochemical and Biophysical Research Communications. 134:915-921 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(86)80507-1 |
| Popis: | T-antigen from SV40-infected BSC-1 cells was purified approximately 30,000 fold using a rapid purification procedure consisting of ammonium sulfate fractionation followed by chromatography on hydroxylapatite, blue-sepharose, and SV40 DNA-sepharose. The SV40 DNA-sepharose was optimized for the binding of T-antigen by the covalent attachment of the SV40 DNA at its BamHI site to cyanogen bromide activated sepharose. The most highly purified T-antigen appeared as a single polypeptide of 94 K daltons by polyacrylamide gel electrophoresis. |
| Databáze: | OpenAIRE |
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