Shiroo M, Kawahara E, Nakanishi I, Migita S
Department of Molecular Immunology, Kanazawa University, Japan.
Scand J Immunol. 1987 Dec;26(6):709-16. doi: 10.1111/j.1365-3083.1987.tb02307.x.
The homogenates of amyloid-laden spleens prepared from CBA mice were analysed by SDS-PAGE and immunoblotting employing rat anti-murine monoclonal antibody, MSA 4-26. The results showed that the precursor of amyloid A protein (AA), serum amyloid A protein 2 (SAA2), and SAA intermediates with molecular weights of 10,000, 9000, and 8000 were contained in amyloid-laden tissues. The experiment using sonicated spleen cells and acute phase murine sera showed a delay in the degradation rate of SAA2 on cell fragments and the remains of SAA1 in supernatants. This result can explain disappearance of SAA2 from the murine serum during amyloidogenesis in vivo.
用来自CBA小鼠制备的富含淀粉样蛋白的脾脏匀浆进行SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)分析,并使用大鼠抗小鼠单克隆抗体MSA 4-26进行免疫印迹分析。结果显示,富含淀粉样蛋白的组织中含有淀粉样蛋白A(AA)蛋白的前体、血清淀粉样蛋白A2(SAA2)以及分子量为10000、9000和8000的SAA中间体。使用超声处理的脾细胞和急性期小鼠血清进行的实验表明,细胞碎片上SAA2的降解速率延迟,上清液中存在SAA1残余物。这一结果可以解释在体内淀粉样蛋白生成过程中SAA2从小鼠血清中的消失。