Purification of factor X by hydrophobic interaction chromatography

Authors
Husi, H Walkinshaw, MD
Citation
H. Husi et Md. Walkinshaw, Purification of factor X by hydrophobic interaction chromatography, J CHROMAT B, 755(1-2), 2001, pp. 367-371
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
JOURNAL OF CHROMATOGRAPHY B
ISSN journal
13872273 → ACNP
Volume
755
Issue
1-2
Year of publication
2001
Pages
367 - 371
Database
ISI
SICI code
1387-2273(20010505)755:1-2<367:POFXBH>2.0.ZU;2-M
Abstract
Human factor X has been purified to homogeneity by hydrophobic interaction chromatography on phenyl-sepharose. The coagulation protein did not interac t with the resin in the presence of 2-3 M NaCl whereas contaminants were re tained. This single purification step, in conjunction with classical purifi cation strategies, is a powerful tool in generating high purity factor X an d is based on resins which are readily available. (C) 2001 Elsevier Science B.V. All rights reserved.