Purification of amyloid protein AA subspecies from amyloid-rich human tissues.
Protein AA, the major amyloid fibril protein in reactive (secondary) systemic amyloidosis is derived from the acute phase reactant liver-produced apolipoprotein serum AA (SAA) by proteolytic cleavage, usually in the C-terminal half of the 104 amino acid residues long precursor. The cleavage points in SAA vary between patients and the deposited protein AA is often quite heterogeneous. In this chapter, we describe methods to extract amyloid fibrils and to purify protein AA by sequential gel filtration. Further purification of subspecies of protein AA is best achieved by the use of differences in charge and chromatofocusing is described as the method of choice. Analytic methods include sodium dodecylsulfate polyacrylamide gel electrophoresis and analytic isoelectric focusing.
Westermark
Gunilla T
GT
Department of Biomedicine and Surgery, Division of Cell Biology, Linköping University, Sweden.
Westermark
Per
P
D006801:Humans; D007525:Isoelectric Focusing / Q000379:methods; D007668:Kidney / Q000378:metabolism; D020033:Protein Isoforms / Q000302:isolation & purification / Q000378:metabolism; D000685:Serum Amyloid A Protein / Q000302:isolation & purification* / Q000378:metabolism; D013154:Spleen / Q000378:metabolism
D020033:Protein Isoforms; D000685:Serum Amyloid A Protein