Linke R P, Bommer J, Ritz E, Waldherr R, Eulitz M
Biochem Biophys Res Commun. 1986 Apr 29;136(2):665-71. doi: 10.1016/0006-291x(86)90492-4.
Urinary stones with amyloid structure, obtained from uremic patients, were analyzed according to molecular weight, amino acid sequence, and antigenic content. A major protein of approximately 7 kD, designated AB protein, was isolated by size exclusion using HPLC in 60% formic acid. AB protein reacted in immunodiffusion only with an antiserum to beta 2-microglobulin, with beta 2m spurring over AB protein. N-terminal amino acid sequence analysis defined two fragments homologous to beta 2m. One fragment commenced with Ile at position 7 and the other with Ser at position 20, with a cleavage point subsequent to a lysyl residue in both. It is concluded that beta 2m is a precursor of urinary amyloid stones and intratubular concretions of patients with preterminal and terminal renal failure; limited proteolysis is involved in AB amyloid generation.
对从尿毒症患者体内获取的具有淀粉样结构的尿结石，按照分子量、氨基酸序列和抗原含量进行了分析。一种约7kD的主要蛋白质，命名为AB蛋白，在60%甲酸中采用高效液相色谱法通过尺寸排阻进行分离。AB蛋白在免疫扩散中仅与抗β2-微球蛋白抗血清发生反应，β2m在AB蛋白上形成刺突。N端氨基酸序列分析确定了与β2m同源的两个片段。一个片段从第7位的异亮氨酸开始，另一个从第20位的丝氨酸开始，两者在赖氨酸残基之后均有一个切割点。得出的结论是，β2m是终末期前和终末期肾衰竭患者尿淀粉样结石和肾小管内结石的前体；有限的蛋白水解参与了AB淀粉样蛋白的生成。
