Husebekk A, Husby G, Sletten K, Marhaug G, Nordstoga K
Scand J Immunol. 1986 Jun;23(6):703-9. doi: 10.1111/j.1365-3083.1986.tb02007.x.
Amyloid was extracted from the liver of a horse that had developed amyloidosis after being used for several years for the production of antibodies to bacterial antigens. The amyloid fibrils were shown to be of the AA type. Two AA proteins with molecular weights of 9000 and 11,000 and with identical partial N-terminal amino acid sequences were identified. Marked structural homology with AA from other species including man was seen, although clear species-related antigenic specificity was observed. SAA isolated from an acute phase (septic abortion) horse serum was identical to AA with respect to antigenicity and the 10 first N-terminal amino acid residues that have been studied up to now. The bulk of SAA was present in the high-density lipoprotein complex in serum. Also SAA was heterogeneous with respect to size, most molecules having a molecular weight of 11,000, and a minority 9000.
