Linke R P, Hampl H, Bartel-Schwarze S, Eulitz M
Biol Chem Hoppe Seyler. 1987 Feb;368(2):137-44. doi: 10.1515/bchm3.1987.368.1.137.
Amyloid deposits of a patient with long-term hemodialysis were immunohistochemically identified as beta 2-microglobulin (beta 2m)-derived. Amyloid proteins were isolated from fibril concentrates from the synovia by HPLC permeation chromatography. Further analysis included dot immunoassay, immunodiffusion, SDS-polyacrylamide gel electrophoresis and Western blotting. Proteins with molecular masses of 8.5, 12, 17 and 24 kDa as well as polymers of higher molecular mass were detected. Neither the 24-kDa dimer nor the higher polymers could be significantly reduced by disulfide reagents. The N-terminal amino-acid sequence analyses of the two major proteins of 12 and 24 kDa showed the same two sequences each: one commencing with position 1 and the other with position 7 of beta 2m. These results suggest that limited proteolysis and polymer formation independent from interchain disulfide bridging, both play a role in the genesis of beta 2m-derived amyloid in the synovia.
一名长期血液透析患者的淀粉样沉积物经免疫组织化学鉴定为源自β2-微球蛋白（β2m）。通过高效液相色谱渗透色谱法从滑膜的纤维浓缩物中分离出淀粉样蛋白。进一步分析包括斑点免疫测定、免疫扩散、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和蛋白质印迹法。检测到分子量为8.5、12、17和24 kDa的蛋白质以及更高分子量的聚合物。二硫试剂无法显著降低24 kDa的二聚体和更高的聚合物。对12 kDa和24 kDa两种主要蛋白质的N端氨基酸序列分析均显示出相同的两个序列：一个从β2m的第1位开始，另一个从第7位开始。这些结果表明，有限的蛋白水解和不依赖链间二硫键桥接的聚合物形成，在滑膜中β2m衍生的淀粉样蛋白的形成过程中均发挥作用。
