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- Rapid and Simple Purification of Biologically Active Human Hepatitis B virus Transactivator-X Proteins
- Poo, Ha Ryoung , Kim, Sun Ok , Sohn, Mi Jin , Lee, Sook , Lee, Young Ik
- J. Microbiol. 1998;36(1):55-58.
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Abstract
- The human hepatitis B virus-X(HBV-X) was cloned into an expression vector, pET3d, containing a T7 promoter and direct expression was induced in Escherichia coli. The expressed HBV-V protein was purified to homogeneity by centrifugation, ion-exchange chromatography and gel filtration. After gel filtration, renaturation of HBV-X were performed using dialysis against serially diluted urea buffer. The biological activity of refolded HBV-X protein was confirmed by enhancement of protein/DNA complexes using gel-shift analysis.
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