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

Producción científica: Article › revisión exhaustiva

5 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	367-371
Número de páginas	5
Publicación	Journal of Chromatography B: Biomedical Sciences and Applications
Volumen	755
N.º	1-2
DOI	https://doi.org/10.1016/S0378-4347(01)00112-8
Estado	Published - 1 may 2001

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10.1016/S0378-4347(01)00112-8

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

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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.",

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AU - Walkinshaw, Malcolm D.

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AB - 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.

U2 - 10.1016/S0378-4347(01)00112-8

DO - 10.1016/S0378-4347(01)00112-8

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JO - Journal of Chromatography B: Biomedical Sciences and Applications

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Purification of factor X by hydrophobic interaction chromatography

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