Résumé
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.
| langue originale | English |
|---|---|
| Pages (de - à) | 367-371 |
| Nombre de pages | 5 |
| journal | Journal of Chromatography B: Biomedical Sciences and Applications |
| Volume | 755 |
| Numéro de publication | 1-2 |
| Les DOIs | |
| état | Published - 1 mai 2001 |