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Purification of factor X by hydrophobic interaction chromatography

By Holger Husi and Malcolm D. Walkinshaw

Abstract

Human factor X has been purified to homogeneity by hydrophobic interaction chromatography on phenyl-sepharose. The coagulation protein did not interact with the resin in the presence of 2-3 M NaCl whereas contaminants were retained. This single purification step, in conjunction with classical purification strategies, is a powerful tool in generating high purity factor X and is based on resins which are readily available

Publisher: Elsevier
Year: 2001
OAI identifier: oai:eprints.gla.ac.uk:128454
Provided by: Enlighten
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