Husby G, Ranløv P J, Sletten K, Marhaug G
Clin Exp Immunol. 1985 Apr;60(1):207-16.
Amyloid obtained from the myocardium of a patient (Han) with familial amyloid cardiomyopathy of Danish origin was studied. Gel filtration and electrophoresis of purified and denatured amyloid fibrils Han revealed various fractions ranging in mol. wt from 40,000 to 8,000 daltons. Amyloid Han and fractions reacted with an antiserum against amyloid Han showing a reaction of identity with each other; partial identity between Han and human pre-albumin was observed, while no reaction was seen with AA or AL proteins. Cardiac tissue sections from Han showed reactivity with antisera to amyloid Han, pre-albumin and protein AP, but not with anti-AA or anti-AL in indirect immunofluorescence. Amino acid composition and sequence studies of a protein fraction of amyloid Han with mol. wt 15,000 daltons confirmed the structural relationship with pre-albumin.
对从一名患有源自丹麦的家族性淀粉样心肌病患者(Han)的心肌中获取的淀粉样蛋白进行了研究。对纯化和变性的淀粉样蛋白原纤维Han进行凝胶过滤和电泳,结果显示其分子量范围为40,000至8,000道尔顿的各种组分。淀粉样蛋白Han及其组分与抗淀粉样蛋白Han抗血清发生反应,彼此显示出同一性反应;观察到Han与人前白蛋白之间存在部分同一性,而与AA或AL蛋白无反应。来自Han的心脏组织切片在间接免疫荧光中与抗淀粉样蛋白Han、前白蛋白和蛋白AP的抗血清发生反应,但与抗AA或抗AL无反应。对分子量为15,000道尔顿的淀粉样蛋白Han的一个蛋白质组分进行氨基酸组成和序列研究,证实了其与前白蛋白的结构关系。