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Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursor
Author(s) -
Ericsson Lowell H.,
Eriksen Nils,
Walsh Kenneth A.,
Benditt Earl P.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81008-6
Subject(s) - residue (chemistry) , amyloidosis , protein primary structure , amino acid residue , peptide sequence , chemistry , amyloid (mycology) , biochemistry , amyloid fibril , amino acid , fibril , peptide , p3 peptide , amyloid precursor protein , amyloid β , pathology , medicine , alzheimer's disease , gene , inorganic chemistry , disease
The amino acid sequence has been determined for the major protein that accumulates in amyloid fibrils in tissues of the Pekin duck. With the exception of 16 residues at the amino terminus, this 106‐residue protein is homologous with human serum amyloid protein A (104‐residue apoSAA), which is the putative precursor of the 76‐residue protein that accumulates in human patients with amyloidosis. Duck serum is shown to contain a protein that is immunologically related and approximately equal in size (12 kDa) to the deposited form in ducks. These results indicate that proteolytic processing of the precursor is not a necessary step in the deposition of amyloid fibrils, at least in the duck.