Recombinant HIV-1 reverse transcriptase: purification, primary structure, and polymerase/ribonuclease H activities.

@article{Mizrahi1989RecombinantHR,
  title={Recombinant HIV-1 reverse transcriptase: purification, primary structure, and polymerase/ribonuclease H activities.},
  author={V Mizrahi and Gary Lazarus and Lynette M. Miles and Claude Meyers and Christine Debouck},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={273 2},
  pages={347-58}
}
Recombinant HIV-1 reverse transcriptase (RT) was stably overproduced as a soluble protein in Escherichia coli using a double-plasmid expression system in which an RT precursor protein was expressed and processed in vivo by HIV-1 protease produced in trans. The RT thus produced consisted of an equimolar mixture of two polypeptides, p66 and p51, which were… CONTINUE READING