Cartwright A J, Morris G E, Love D R, Bloomfield J F, Davies K E
Research Division, N.E. Wales Institute, Deeside, Clwyd, U.K.
FEBS Lett. 1990 Mar 26;262(2):237-40. doi: 10.1016/0014-5793(90)80199-s.
Nineteen monoclonal antibodies which bind to native dystrophin in the plasma membrane of frozen muscle sections were obtained using a recombinant fusion protein as immunogen. On Western blots of normal mouse muscle extracts, the antibodies bind specifically to a 400,000 Mr protein which is absent from dystrophic mouse (mdx) muscle. At least four distinct epitopes have been identified by cleavage mapping methods. Although the fusion protein contained 25% of the human dystrophin sequence (Cys816-Asp1747; Mr 108,000), most of the monoclonal antibodies (15 out of 19) recognize a single fragment of Mr 27,500.
以重组融合蛋白作为免疫原，获得了19种可与冷冻肌肉切片质膜中的天然抗肌萎缩蛋白结合的单克隆抗体。在正常小鼠肌肉提取物的蛋白质免疫印迹分析中，这些抗体特异性结合一种分子量为400,000的蛋白质，而这种蛋白质在营养不良小鼠（mdx）的肌肉中不存在。通过裂解图谱法已鉴定出至少四个不同的表位。尽管融合蛋白包含25%的人抗肌萎缩蛋白序列（Cys816 - Asp1747；分子量108,000），但大多数单克隆抗体（19种中的15种）识别的是一个分子量为27,500的单一片段。
