| Literature DB >> 2597108 |
A F Strachan1, E G Shephard, D U Bellstedt, G A Coetzee, D R van der Westhuyzen, F C de Beer.
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 (greater than 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 greater than 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.Entities:
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Year: 1989 PMID: 2597108 PMCID: PMC1133438 DOI: 10.1042/bj2630365
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857