Title Rapid and Simple Purification of Biologically Active Human Hepatitis B virus Transactivator-X Proteins
Author Poo, Ha Ryoung · Kim, Sun Ok · Sohn, Mi Jin · Lee, Sook · Lee, Young Ik *
Address Liver Cell signal Tranduction Research Unit, Korea Research Institute of Bioscience and Biotechnology, Korea Institute of Science and Technologym Daeduck Science Town
Bibliography Journal of Microbiology, 36(1),55-58, 1998,
DOI
Key Words Hepatitis B virus-X protein, expression, purification
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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