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

科研成果: Article › 同行评审

5 引用（Scopus）

摘要

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.

源语言	English
页（从-至）	367-371
页数	5
期刊	Journal of Chromatography B: Biomedical Sciences and Applications
卷	755
期	1-2
DOI	https://doi.org/10.1016/S0378-4347(01)00112-8
出版状态	Published - 1 5月 2001

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10.1016/S0378-4347(01)00112-8

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

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Purification of factor X by hydrophobic interaction chromatography

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