Isoforms of Recombinant Human Erythropoietin

  • R. V. Battersby
  • B. Ohlrogge
  • A. Feigler
  • C. J. Holloway
Conference paper


Recombinant human erythropoietin (rHuEPO) has been made commercially available utilizing a variety of expression systems. Whereas the peptide backbones of these recombinant proteins can be expected to be identical, a polymorphism of these recombinant materials with distinct variations in biological and physicochemical properties is observed. This is related to extensive posttranslational modification processes, which add complex oligosaccharide side chains to the molecule, amounting to approx. 40% of the total molecular mass.


Chinese Hamster Ovary Cell Recombinant Human Erythropoietin Relative Molecular Mass Sugar Chain Recombinant Erythropoietin 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • R. V. Battersby
  • B. Ohlrogge
  • A. Feigler
  • C. J. Holloway

There are no affiliations available

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