title: Purification of factor X by hydrophobic interaction chromatography.
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.
authors.affiliation: Centre for Genome Research, The University of Edinburgh, UK. hhusi@srv0.bio.ed.ac.uk
authors.forename: H
authors.initials: H
authors.lastname: Husi
authors.forename: M D
authors.initials: MD
authors.lastname: Walkinshaw
mesh_terms: D001779:Blood Coagulation Factors / Q000737:chemistry*; D002845:Chromatography / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D005170:Factor X / Q000302:isolation & purification*; D006801:Humans; D012685:Sepharose / Q000031:analogs & derivatives
chemical_list: D001779:Blood Coagulation Factors; C037405:heparin-sepharose; C020927:phenyl-sepharose; D005170:Factor X; D012685:Sepharose