Purification of factor X by hydrophobic interaction chromatography

Holger Husi, Malcolm D. Walkinshaw

Research output: Contribution to journalArticle

4 Citations (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.
Original languageEnglish
Pages (from-to)367-371
Number of pages5
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Volume755
Issue number1-2
DOIs
Publication statusPublished - 1 May 2001

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