Sletten K, Westermark P, Natvig J B
Scand J Immunol. 1980;12(6):503-6. doi: 10.1111/j.1365-3083.1980.tb00098.x.
The major component, protein ASC, isolated from the amyloid fibrils in senile cardiac amyloidosis, was characterized by structural studies of some peptic peptides. One of the peptides has an amino acid sequence identical to residues 70-90 in human prealbumin, and three other smaller peptides have a primary structure identical to that in positions 96-107, 109-115 and 121-127. The amino acid composition of the protein resembles that of human prealbumin but shows some characteristic differences. The protein has a blocked N-terminus and gives no visible precipitin reaction with antiserum to human prealbumin.
从老年心脏淀粉样变性的淀粉样原纤维中分离出的主要成分蛋白质ASC，通过对一些胃蛋白酶消化肽的结构研究进行了表征。其中一种肽的氨基酸序列与人前白蛋白的70-90位残基相同，另外三种较小的肽的一级结构与96-107、109-115和121-127位的结构相同。该蛋白质的氨基酸组成与人前白蛋白相似，但显示出一些特征性差异。该蛋白质的N端被封闭，与抗人前白蛋白血清无明显沉淀反应。
