Isolation and structural properties of murine SAA--the acute phase serum precursor of amyloid AA.
The murine serum protein SAA, has been found to have a structure similar to human SAA, the precursor of human secondary amyloid fibril protein AA. SAA is detected by its cross-reaction in radioimmunoassay with antibodies raised to denatured amyloid fibrils of protein AA isolated from tissues of mice with amyloidosis. Murine SAA exists in the native state as a 160,000 molecular weight species, and can be isolated as a 12,500 molecular weight moiety, SAAL, by gel filtration in 10% formic acid. The quaternary structure of SAA is such that its AA determinants are relatively inaccessible for immunoreaction. Unfolding of these determinants can occur spontaneously; however, it is promoted by dissociation of SAA to SAAL.
D000682:Amyloid / Q000097:blood / Q000302:isolation & purification*; D000686:Amyloidosis / Q000097:blood; D000818:Animals; D001797:Blood Protein Electrophoresis; D001798:Blood Proteins / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice / Q000097:blood*; D008970:Molecular Weight; D011487:Protein Conformation; D011498:Protein Precursors / Q000302:isolation & purification*; D011863:Radioimmunoassay
D000682:Amyloid; D001798:Blood Proteins; D011498:Protein Precursors