Costa P P, Figueira A S, Bravo F R
Proc Natl Acad Sci U S A. 1978 Sep;75(9):4499-503. doi: 10.1073/pnas.75.9.4499.
Amyloid fibrils were concentrated from the kidney, thyroid, and peripheral nerve of six patients with familial amyloidotic polyneuropathy (FAP). The fibril concentrates were solubilized in 6 M guanidine.HCl and fractionated on Sephadex G-100 columns. The elution profile of all FAP amyloid fibril concentrates revealed a protein of apparent Mr of 14,000, designated the FAP protein, that was absent from normal human tissues treated by the same procedure and from fibrils of a primary amyloidosis liver. Antisera against whole denatured fibril concentrates prepared in rabbits reacted with the FAP protein and a component in normal human serum corresponding to prealbumin. It was further established that the FAP protein shared common antigenic determinants with human prealbumin by its reaction of identity with normal prealbumin using commercial antisera against human prealbumin. Amyloid AL or AA proteins could not be identified in FAP fibrils by sensitive immunochemical assay methods. These results suggest that the FAP protein is a unique and significant component of the FAP amyloid fibrils and that it is closely related to the 13,745 Mr prealbumin subunit.
从6例家族性淀粉样多神经病（FAP）患者的肾脏、甲状腺和周围神经中富集淀粉样原纤维。将原纤维浓缩物溶解于6M盐酸胍中，并在葡聚糖G - 100柱上进行分级分离。所有FAP淀粉样原纤维浓缩物的洗脱图谱显示出一种表观分子量为14,000的蛋白质，命名为FAP蛋白，在经过相同处理的正常人体组织以及原发性淀粉样变性肝病的原纤维中均不存在。用兔制备的针对全变性原纤维浓缩物的抗血清与FAP蛋白以及正常人血清中对应于前白蛋白的一种成分发生反应。通过使用针对人前白蛋白的商业抗血清，FAP蛋白与正常前白蛋白的同一性反应进一步证实FAP蛋白与人类前白蛋白具有共同的抗原决定簇。通过灵敏的免疫化学检测方法在FAP原纤维中未鉴定出淀粉样AL或AA蛋白。这些结果表明FAP蛋白是FAP淀粉样原纤维的一种独特且重要的成分，并且它与分子量为13,745的前白蛋白亚基密切相关。
