Recombinant human hemoglobin: Expression and refolding of β-globin from Escherichia coli

Clara Fronticelli, J. Kevin O'Donnell, William S. Brinigar

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


A plasmid analogous to the one described by Nagai and Thogersen (Nature, 309, 810-812, 1984) has been constructed for the expression of globins in E. coli. Induction with nalidixic acid produces high yields of a fusion protein, NS1-FX-β-globin, where NS1 represents 81 residues of a flu virus protein and FX represents a blood-clotting Factor Xa recognition sequence, Ile-Glu-Gly-Arg. This fusion protein is readily solubilized in 50 mM NaOH and remains in solution when the pH is adjusted to 8.6. Under these conditions, the fusion protein is hydrolyzed by activated Factor X, giving authentic β-globin which can be folded in the presence of cyanohemin and native α-chains to produce a tetrameric hemoglobin with the functional properties of natural human hemoglobin.

Original languageEnglish (US)
Pages (from-to)495-501
Number of pages7
JournalJournal of Protein Chemistry
Issue number5
StatePublished - Oct 1991
Externally publishedYes


  • Hemoglobin
  • protein folding
  • recombinant hemoglobin

ASJC Scopus subject areas

  • Biochemistry


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