Recombinant human erythropoietin: Purification and analysis of carbohydrate linkage

Virginia C. Broudy, Jonathan F. Tait, Jerry S Powell

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Erythropoietin was purified to homogeneity from the culture medium of a baby hamster kidney cell line stably transfected with a human erythropoietin gene. A three-step procedure was used, which included affinity chromatography, ion-exchange chromatography, and reverse-phase chromatography. Purity of the protein was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino-terminal sequence analysis. Overall recovery was 35%. The biological activity of purified recombinant erythropoietin was similar to that of the native hormone in vitro. The purified recombinant hormone contained N-linked carbohydrate at residues 24, 38, and 83, and an O-linked carbohydrate at residue 126.

Original languageEnglish (US)
Pages (from-to)329-336
Number of pages8
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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