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.
|Number of pages||5|
|Journal||Journal of Chromatography B: Biomedical Sciences and Applications|
|Publication status||Published - 1 May 2001|
Husi, H., & Walkinshaw, M. D. (2001). Purification of factor X by hydrophobic interaction chromatography. Journal of Chromatography B: Biomedical Sciences and Applications, 755(1-2), 367-371. https://doi.org/10.1016/S0378-4347(01)00112-8