Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production
Date
1989
Authors
Strachan A.F.
Shephard E.G.
Bellstedt D.U.
Coetzee G.A.
Van Der Westhuyzen D.R.
De Beer F.C.
Journal Title
Journal ISSN
Volume Title
Publisher
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.
Description
Keywords
amyloid a protein, isoprotein, urea, amyloid a protein blood level, human, priority journal, protein structure, Adsorption, Amyloid Protein SAA, Antibodies, Antigens, Electrophoresis, Polyacrylamide Gel, Human, Hydrogen-Ion Concentration, Immunization, Isoelectric Point, Lipoproteins, HDL, Protein Conformation, Salmonella, Solubility, Solutions, Support, Non-U.S. Gov't, Urea, Water
Citation
Biochemical Journal
263
2
263
2