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 2-3M 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 |
|---|---|
| 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 - 5 May 2001 |
| Externally published | Yes |
Free Keywords
- Factor X
- Purification
ASJC Scopus subject areas
- General Chemistry
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