Expression, purification, and characterization of authentic monoferric and apo-human serum transferrins.

@article{Mason2004ExpressionPA,
  title={Expression, purification, and characterization of authentic monoferric and apo-human serum transferrins.},
  author={Anne B Mason and Peter J Halbrooks and Julia R. Larouche and Sara K Briggs and Marque L Moffett and Jon E Ramsey and Susan A Connolly and Valerie C. Smith and R. T. MacGillivray},
  journal={Protein expression and purification},
  year={2004},
  volume={36 2},
  pages={318-26}
}
Transferrin is a bilobal protein with the ability to bind iron in two binding sites situated at the bottom of a cleft in each lobe. We have previously described the production of recombinant non-glycosylated human serum transferrins (hTF-NG), containing a factor Xa cleavage site and a hexa-His tag at the amino-terminus. Constructs in this background that… CONTINUE READING