Purification of transferrin from Cohn supernatant I using ion-exchange chromatography

Karl B. McCann, Ben Hughes, John Wu, Joseph Bertolini, Peter T. Gomme

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


The present paper describes an anion-exchange chromatography method to separate iron-free apo-Tf (apo-transferrin) from albumin and IgG in Cohn supernatant I. The method uses DEAE-fast flow Sepharose chromatography along with optimized protein concentration (5%, w/v) and column operation conditions (40 g/l, conductivity < 1.0 mS/cm) to resolve apo-Tf from IgG and albumin. The single step purifies apo-Tf to > 90% and provides an efficient means to obtain commercial quantities of the protein.

Original languageEnglish
Pages (from-to)211-217
Number of pages7
JournalBiotechnology and Applied Biochemistry
Issue number3
Publication statusPublished - Dec 1 2005
Externally publishedYes


  • Cohn supernatant I
  • Human serum albumin (HSA)
  • Ion-exchange chromatography
  • Iron transport
  • Plasma
  • Transferrin

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Molecular Medicine
  • Biomedical Engineering
  • Applied Microbiology and Biotechnology
  • Drug Discovery
  • Process Chemistry and Technology


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