Chromatographic purification of recombinant human erythropoietin.


Department of Chemical and Biochemical Engineering, Faculty of Chemical and Food Technology, Institute of Chemical and Environmental Engineering, Slovak University of Technology, Radlinského 9, 812 37, Bratislava, Slovakia. [Email]


Recombinant human erythropoietin is a valuable therapeutic protein used in the treatment of several serious diseases. It exists in different isoforms and is produced by genetically modified mammalian cells such as Chinese hamster ovary or human embryonic kidney cells. As for other biopharmaceutical drugs, a key factor for its successful industrial production is to achieve a high degree of purity and to decrease the content of critical impurities to trace amounts. This goal is achieved in the separation sequence which substantial part is formed by chromatographic steps. Therefore, downstream processing forms an essential part of production costs. This review presents the overview of published separation sequences and, analyzes the use of different types of chromatographic media such as affinity, ion-exchange, reversed-phase, hydrophobic interaction, multimodal, and size-exclusion chromatography adsorbents. Their application is discussed with regard to their place in the purification stages generally denoted as capture, intermediate purification and polishing.


Downstream processing,Purification,Recombinant human erythropoietin,Separation procedure,Therapeutic protein,

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