Characterization of bovine amyloid proteins SAA and AA.
The bovine serum amyloid A (SAA) and tissue amyloid A (AA) proteins were isolated and characterized. SAA was isolated from acute phase high density lipoprotein (HDL) of a cow suffering from acute mastitis, and was identified by amino acid sequence analysis. No AA-like protein was found in complex with HDL in serum. Amyloid fibrils isolated from a bovine kidney contained a 9 kDa AA protein and a considerable amount of a 14 kDa protein. Amino acid sequence analysis showed that the largest protein probably represents undegraded SAA. This is an interesting observation which confirms previous works indicating that SAA can be incorporated in the amyloid fibrils without a prior degradation to AA. The partial amino acid sequences of bovine SAA and AA were strikingly homologous to the sequences of corresponding proteins in man and other species.
Husebekk
A
A
Department of Rheumatology, University of Tromsø, Norway.
Husby
G
G
Sletten
K
K
Skogen
B
B
Nordstoga
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle / Q000097:blood*; D008075:Lipoproteins, HDL / Q000032:analysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments; D000685:Serum Amyloid A Protein / Q000302:isolation & purification*
D008075:Lipoproteins, HDL; D010446:Peptide Fragments; D000685:Serum Amyloid A Protein