Abstract
Coagulation factor VIII is one of the largest proteins attempted to be expressed in recombinant form. A very complex and labile protein which has a very short half-live and need a fast and efficient purification chain. Here, we describe a simple purification sequence using multimodal Capto MMC, affinity FVIII select and ion exchange SP-Fastflow chromatography steps without subjecting the target molecule to mechanical and temperature stress, separating impurities from rFVIII using net charge, hydrophobicity, and affinity of the molecules.
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Granovski, V., Abreu-Neto, M.S., Covas, D.T. (2018). Purification Methods for Recombinant Factor VIII Expressed in Human Liver SK-Hep Cells. In: Picanço-Castro, V., Swiech, K. (eds) Recombinant Glycoprotein Production. Methods in Molecular Biology, vol 1674. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7312-5_15
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DOI: https://doi.org/10.1007/978-1-4939-7312-5_15
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Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-7311-8
Online ISBN: 978-1-4939-7312-5
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