Structural Studies of SAA and AA from Horse and Cow
Horse and bovine serum amyloid protein A (SAA) and tissue amyloid A (AA) were isolated,and their primary structure were compared to the known amino acid sequences of SAA and AA from mink and man (1,2,3,4).
Both horse and bovine SAA were isolated from acute phase HDL and part of the N-terminal amino acid sequences of the proteins are presented.Further studies of the total amino acid sequence of horse SAA have given indications for three microhet-erogeneities. Horse AA consists of 80 amino acid residues (5) and a heterogeneity was observed in position 44.The known sequence of bovine AA is homologous to that of SAA.
These amino acid sequences are discussed together with the known sequences of human and mink SAA and AA with respect to properties making the proteins prone to amyloid fibril formation.
KeywordsHigh Density Lipoprotein Amyloid Fibril Amyloid Protein Cyanogen Bromide Acute Phase Serum
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