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.
Original language | English |
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Pages (from-to) | 367-371 |
Number of pages | 5 |
Journal | Journal of Chromatography B: Biomedical Sciences and Applications |
Volume | 755 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1 May 2001 |