Westermark P, Sletten K, Olofsson B O
Department of Pathology, Uppsala University, Sweden.
Clin Exp Immunol. 1987 Sep;69(3):695-701.
Amino-acid sequence analysis of an amyloid fibril protein from a patient with Swedish familial amyloidotic polyneuropathy showed homology with prealbumin but with heterogeneous N-terminal deletions. One-third of the molecules had the same amino acid substitution, methionine for valine in position 30, as in familial amyloidosis of Portuguese, Japanese and Swedish-American type. A protein with the same antigenic properties and size was found in the fibrils of two other patients with Swedish FAP while the amyloid fibrils in two further patients predominantly contained a smaller prealbumin-derived protein. Cyanogen bromide cleavage of this protein revealed no evidence for a methionine residue in position 30.
对一名患有瑞典家族性淀粉样多神经病患者的淀粉样纤维蛋白进行氨基酸序列分析，结果显示其与前白蛋白具有同源性，但N端存在异质性缺失。三分之一的分子具有相同的氨基酸替代，即第30位的缬氨酸被甲硫氨酸替代，这与葡萄牙型、日本型和瑞典裔美国型家族性淀粉样变性相同。在另外两名患有瑞典型家族性淀粉样多神经病患者的纤维中发现了具有相同抗原特性和大小的蛋白质，而另外两名患者的淀粉样纤维主要含有一种较小的前白蛋白衍生蛋白。对该蛋白进行溴化氰裂解，未发现第30位存在甲硫氨酸残基的证据。
