Purification of factor X by hydrophobic interaction chromatography

Holger Husi; Malcolm D. Walkinshaw

doi:10.1016/S0378-4347(01)00112-8

Purification of factor X by hydrophobic interaction chromatography

Holger Husi
, Malcolm D. Walkinshaw

Division of Biomedical Sciences

Publikation › Begutachtung

5 Zitate (Scopus)

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.

Originalsprache	English
Seiten (von - bis)	367-371
Seitenumfang	5
Fachzeitschrift	Journal of Chromatography B: Biomedical Sciences and Applications
Jahrgang	755
Ausgabenummer	1-2
DOIs	https://doi.org/10.1016/S0378-4347(01)00112-8
Publikationsstatus	Published - 1 Mai 2001

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10.1016/S0378-4347(01)00112-8

http://eprints.gla.ac.uk/128454/

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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.",

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Purification of factor X by hydrophobic interaction chromatography

Abstract

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