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 language | English |
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Pages (from-to) | 365-370 |
Number of pages | 6 |
Journal | Biochemical Journal |
Volume | 263 |
Issue number | 2 |
DOIs | |
State | Published - 1989 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology