Dang H, Fischbach M, Lerner E, Talal N
J Immunol. 1983 Jun;130(6):2782-5.
The Sm antigen was isolated and purified from calf thymus nuclear extract by affinity chromatography. The affinity columns were made with serum antibodies from an SLE patient or an anti-Sm monoclonal antibody derived from a hybridoma cell line. Proteins eluted from these two columns had m.w. of 58,000 and 35,000 by SDS polyacrylamide gel electrophoresis. The natural conformation of this antigen appears to be 95,000 in m.w. with the 58,000 particle containing the Sm antigenic determinant. The affinity column-purified antigen detected by the human anti-Sm antibodies is also recognized by anti-Sm antibodies in murine lupus serum, as shown by solid-phase radioimmunoassay. This study 1) demonstrates the molecular and antigenic nature of the Sm antigen and 2) compares the anti-Sm binding capabilities of antibody populations present in sera from SLE patients and from MRL lpr/lpr mice.
通过亲和层析从小牛胸腺核提取物中分离并纯化了Sm抗原。亲和柱是用来自一名系统性红斑狼疮（SLE）患者的血清抗体或源自杂交瘤细胞系的抗Sm单克隆抗体制备的。通过SDS聚丙烯酰胺凝胶电泳，从这两种柱上洗脱下来的蛋白质分子量分别为58,000和35,000。该抗原的天然构象分子量似乎为95,000，其中58,000的颗粒含有Sm抗原决定簇。固相放射免疫分析表明，人抗Sm抗体检测到的亲和柱纯化抗原也能被鼠狼疮血清中的抗Sm抗体识别。本研究1）证明了Sm抗原的分子和抗原性质，2）比较了SLE患者血清和MRL lpr/lpr小鼠血清中抗体群体的抗Sm结合能力。
