High-yield expression in Escherichia coli of soluble human alpha-hemoglobin complexed with its molecular chaperone.

@article{VasseurGodbillon2006HighyieldEI,
  title={High-yield expression in Escherichia coli of soluble human alpha-hemoglobin complexed with its molecular chaperone.},
  author={Corinne Vasseur-Godbillon and Djemel Hamdane and M C Michael C Marden and V{\'e}ronique Baudin-Creuza},
  journal={Protein engineering, design & selection : PEDS},
  year={2006},
  volume={19 3},
  pages={91-7}
}
The alpha-subunits of human hemoglobin (Hb) have been more difficult to express than beta-chains owing to the high instability of alpha-chains. Here, we describe the production in Escherichia coli of a soluble recombinant alpha-Hb with human alpha-hemoglobin-stabilizing protein (AHSP), its molecular chaperone. To succeed in this expression, we have constructed a vector pGEX-alpha-AHSP which contains two cassettes arranged in tandem in the same orientation permitting to express alpha-hemoglobin… CONTINUE READING

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