%0 Journal Article
%T Active recombinant Reverse Transcriptase Domain of human Hepatitis B Virus Polymerase
%A Dipendra Raj P
%A Seong-Tshool Hong
%A Yu Yang
%A eya
%J -
%D 2011
%X Hepatitis B virus polymerase plays a critical role during HBV life cycle, and polymerase/reverse transcriptase (RT) activities are critical for HBV-pol during viral replication. To investigate RT do-main of human HBV polymerase, a 5กฏ end Polyhistidine tagged RT DNA (304-693 amino acids) of HBV-pol was successfully expressed in Escherichia coli. Recombinant RT was purified in native condition employing Ni-NTA affinity column. Purified RT showed a stable reverse transcriptase ac-tivity and a much stronger DNA polymerase activity, compared to RT expressed in rabbit reticulo-cyte lysate coupled transcriptase-translation system. We present a new simplified way of obtaining active RT protein using the Escherichia coli expression and Reticulocyte lysate system. The purified RT was a stable protein and showed a low selective polymerase activity. Computer modeling results also indicated that RT domain banded to nucleotide substrate in a loose mode
%K Hepatitis B Virus
%K polymerase
%K reverse transcriptase
%K detergent
%U https://www.alliedacademies.org/articles/active-recombinant-reverse-transcriptase-domain-of-human-hepatitis-b-virus-polymerase.html