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鸭淀粉样蛋白A的一级结构。沉积于组织中的形式可能与其血清前体相同。

Primary structure of duck amyloid protein A. The form deposited in tissues may be identical to its serum precursor.

作者信息

Ericsson L H, Eriksen N, Walsh K A, Benditt E P

出版信息

FEBS Lett. 1987 Jun 22;218(1):11-6. doi: 10.1016/0014-5793(87)81008-6.

DOI:10.1016/0014-5793(87)81008-6
PMID:3109944
Abstract

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.

摘要

已确定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。除了氨基末端的16个残基外,这种106个残基的蛋白质与人类血清淀粉样蛋白A(104个残基的载脂蛋白SAA)同源,后者是在人类淀粉样变性患者中积累的76个残基蛋白质的推定前体。鸭血清显示含有一种与鸭子体内沉积形式免疫相关且大小近似(12 kDa)的蛋白质。这些结果表明,前体的蛋白水解加工至少在鸭体内不是淀粉样原纤维沉积的必要步骤。

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