Characterisation of recombinant unglycosylated human serum transferrin purified from Saccharomyces cerevisiae

Peter J. Sargent, Sebastien Farnaud, Richard Cammack, Heinz M P Zoller, Robert W. Evans

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Structural identity between a recombinant transferrin mutant (N413Q, N611Q) secreted from Saccharomyces cerevisiae and the native protein was shown by CD analysis and immunodiffusion assays against anti-hSTf. The ability of the recombinant protein to bind iron was confirmed by urea-PAGE and EPR analysis of the iron-saturated protein revealed the characteristic holo-transferrin spectrum, indicating conservation of both iron-binding sites. The integrity of the unglycosylated recombinant protein indicates that such protein could be a valuable tool not only for structure-function characterisation but also crystallisation assays. In addition, the recombinant transferrin was found to be as effective as native transferrin as a growth factor in cell culture medium.

Original languageEnglish
Pages (from-to)513-519
Number of pages7
Issue number5
Publication statusPublished - Oct 2006
Externally publishedYes


  • Characterisation
  • Iron
  • Recombinant
  • Saccharomyces cerevisiae
  • Transferrin
  • Yeast

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)


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