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 Citations (Scopus)

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

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Serum Amyloid A Protein
Chromatography
Hydrophobic and Hydrophilic Interactions
Purification
Ethanol
formic acid
Serum
Acute-Phase Proteins
Apolipoproteins
Guanidine
Gel Chromatography
Urea
Gels
Recovery

ASJC Scopus subject areas

  • Biotechnology

Cite this

Use of ethanol-eluted hydrophobic interaction chromatography in the purification of serum amyloid A. / Smith, James W.; McDonald, Thomas L.

In: Protein Expression and Purification, Vol. 2, No. 2-3, 01.01.1991, p. 158-161.

Research output: Contribution to journalArticle

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