Skip to main navigation Skip to search Skip to main content

Purification of factor X by hydrophobic interaction chromatography

  • Holger Husi*
  • , Malcolm D. Walkinshaw
  • *Corresponding author for this work

Research output: Journal PublicationArticlepeer-review

5 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 2-3M 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 - 5 May 2001
Externally publishedYes

Free Keywords

  • Factor X
  • Purification

ASJC Scopus subject areas

  • General Chemistry

Fingerprint

Dive into the research topics of 'Purification of factor X by hydrophobic interaction chromatography'. Together they form a unique fingerprint.

Cite this