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  • Title: Isolation and structural properties of murine SAA--the acute phase serum precursor of amyloid AA.
    Author: Sipe JD, McAdam KP, Torain BF, Pollock PS.
    Journal: Immunol Commun; 1977; 6(1):1-12. PubMed ID: 863470.
    Abstract:
    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.
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