Purification of factor X by hydrophobic interaction chromatography

Husi, H. and Walkinshaw, M. D. (2001) Purification of factor X by hydrophobic interaction chromatography. Journal of Chromatography B: Biomedical Sciences and Applications, 755(1-2), pp. 367-371. (doi:10.1016/S0378-4347(01)00112-8) (PMID:11393727)

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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.

Item Type:Articles (Other)
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Husi, Dr Holger
Authors: Husi, H., and Walkinshaw, M. D.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cardiovascular and Medical Sciences
Journal Name:Journal of Chromatography B: Biomedical Sciences and Applications
Publisher:Elsevier
ISSN:1387-2273
Published Online:12 April 2001

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