Use of ethanol-eluted hydrophobic interaction chromatography in the purification of serum amyloid A

James W. Smith, Thomas L. McDonald

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A two-step procedure for the purification of the acute-phase reactant serum amyloid A from serum is described. A hydrophobic interaction chromatography medium, octyl-Sepharose CL4B, eluted with increasing concentrations of EtOH was used as the first step in the purification. The concentrate from this step was applied to a gel filtration column of Sephacryl S-200 and eluted with 10% formic acid. The overall recovery of purified serum amyloid A from serum was 56%. This represents the first time that serum amyloid A has been purified without the use of high concentrations of guanidine or urea. The method presented could easily be scaled up to allow the purification of large quantities of serum amyloid A or readily adapted to the purification of other serum apolipoproteins.

Original languageEnglish (US)
Pages (from-to)158-161
Number of pages4
JournalProtein Expression and Purification
Volume2
Issue number2-3
DOIs
StatePublished - Jan 1 1991

ASJC Scopus subject areas

  • Biotechnology

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