Rapid and simple purification of biologically active human hepatitis B virus transactivator-X proteins

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Title
Rapid and simple purification of biologically active human hepatitis B virus transactivator-X proteins
Author(s)
Ha Ryoung Poo; Sun Ok Kim; Mi Jin Sohn; Sook Lee; Young Ik Lee
Bibliographic Citation
Journal of Microbiology, vol. 36, no. 1, pp. 55-58
Publication Year
1998
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-X 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.
Keyword
expressionpurificationHepatitis B virus-X protein
ISSN
1225-8873
Publisher
Microbiological Society Korea
Type
Article
Appears in Collections:
Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
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