Gorevic P D, Casey T T, Stone W J, DiRaimondo C R, Prelli F C, Frangione B
J Clin Invest. 1985 Dec;76(6):2425-9. doi: 10.1172/JCI112257.
Curvilinear fibrils with the tinctorial properties of amyloid were isolated from a patient with bone and joint involvement complicating chronic dialysis for renal disease. Subunit fractions of 24,000 and 12,000 mol wt were identified after gel filtration under dissociating conditions, the latter containing a significant amount of a dimer of the former. This was confirmed by Edman degradation of each fraction, which yielded the amino terminal sequence of normal human beta-2 microglobulin (B2M) to residues 20 and 30, respectively. The size of the subunit protein (12,000 mol wt) and the amino acid composition make it likely that intact B2M is a major constituent of the fibrils. B2M is thus another example of a low molecular weight serum protein, with a prominent beta-pleated sheet structure, that may adopt the fibrillar configuration of amyloid in certain pathologic states.
从一名患有因肾病而慢性透析并发骨和关节受累的患者身上分离出具有淀粉样蛋白染色特性的曲线形原纤维。在解离条件下进行凝胶过滤后，鉴定出分子量为24,000和12,000的亚基组分，后者含有大量前者的二聚体。通过对每个组分进行埃德曼降解证实了这一点，其分别产生了正常人β-2微球蛋白（B2M）至第20和30位残基的氨基末端序列。亚基蛋白的大小（12,000分子量）和氨基酸组成表明完整的B2M可能是原纤维的主要成分。因此，B2M是另一个低分子量血清蛋白的例子，其具有突出的β-折叠结构，在某些病理状态下可能呈现淀粉样蛋白的纤维状结构。
