Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

A. F. Strachan, E. G. Shephard, D. U. Bellstedt, G. A. Coetzee, D. R. Van Der Westhuyzen, F. C. De Beer

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

Original languageEnglish
Pages (from-to)365-370
Number of pages6
JournalBiochemical Journal
Volume263
Issue number2
DOIs
StatePublished - 1989

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production'. Together they form a unique fingerprint.

Cite this