PRIMARY STRUCTURE OF DUCK AMYLOID PROTEIN-A - THE FORM DEPOSITED IN TISSUES MAY BE IDENTICAL TO ITS SERUM PRECURSOR
PRIMARY STRUCTURE OF DUCK AMYLOID PROTEIN-A - THE FORM DEPOSITED IN TISSUES MAY BE IDENTICAL TO ITS SERUM PRECURSOR
复制标题
DOI：
10.1016/0014-5793(87)81008-6
复制
发表时间：
1987-06-22
期刊：
影响因子：
3.5
通讯作者：
BENDITT, EP
中科院分区：
文献类型：
--
作者：
ERICSSON, LH;ERIKSEN, N;BENDITT, EP
北京鸭组织中淀粉样原纤维中积累的主要蛋白质的氨基酸序列已被确定。除了氨基末端的 16 个残基外，该 106 个残基蛋白与人血清淀粉样蛋白 A（104 个残基 apoSAA）同源，后者是人类淀粉样变性患者体内积累的 76 个残基蛋白的假定前体。鸭血清显示含有一种与免疫学相关的蛋白质，其大小 (12 kDa) 与鸭体内沉积形式大致相同。这些结果表明，前体的蛋白水解加工不是淀粉样原纤维沉积的必要步骤，至少在鸭中是这样。
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.