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.
CITATION STYLE
Granovski, V., Abreu-Neto, M. S., & Covas, D. T. (2018). Purification methods for recombinant factor VIII expressed in human liver SK-Hep cells. In Methods in Molecular Biology (Vol. 1674, pp. 195–202). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7312-5_15
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