Yonezu T, Higuchi K, Tsunasawa S, Takagi S, Sakiyama F, Takeda T
FEBS Lett. 1986 Jul 28;203(2):149-52. doi: 10.1016/0014-5793(86)80732-3.
The primary structure of a murine senile amyloid protein (ASSAM) was determined. The protein consists of a single polypeptide chain of 78 amino acid residues. The amino-terminus is blocked with pyrrolidone-carboxylic acid. The sequence differs from that of the known murine amyloid A protein and is highly homologous to human apolipoprotein (apo) A-II. The result indicates that the putative precursor of the senile amyloid protein is apo A-II in mice.
确定了一种小鼠老年性淀粉样蛋白(ASSAM)的一级结构。该蛋白由一条含78个氨基酸残基的单多肽链组成。氨基末端被吡咯烷酮羧酸封闭。其序列与已知的小鼠淀粉样蛋白A不同,与人类载脂蛋白(apo)A-II高度同源。结果表明,小鼠老年性淀粉样蛋白的假定前体是apo A-II。