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.
Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production
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A F Strachan, E G Shephard, D U Bellstedt, G A Coetzee, D R van der Westhuyzen, F C de Beer; Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production. Biochem J 15 October 1989; 263 (2): 365–370. doi: https://doi.org/10.1042/bj2630365
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