Nguyen T M, Ellis J M, Ginjaar I B, van Paassen M M, van Ommen G J, Moorman A F, Cartwright A J, Morris G E
Research Division, NE Wales Institute, Deeside, Clwyd, UK.
FEBS Lett. 1990 Oct 15;272(1-2):109-12. doi: 10.1016/0014-5793(90)80460-z.
A monoclonal antibody, MANDYS141, binds to both dystrophin and actinin on Western blots (SDS-denatured), but only to actinin in frozen sections of human muscle (native conformation). It differs from a polyclonal cross-reacting antiserum in that it binds to several muscle isoforms of actinin (smooth, fast and slow) from man, mouse and chicken and recognises a quite different part of the proposed triple-helical region of dystrophin (amino acids 1750-2248). The results suggest that structural homologies between actinin and dystrophin occur more than once in their central helical regions and provide experimental support for an actinin-like central rod model for dystrophin.
一种单克隆抗体MANDYS141，在蛋白质免疫印迹法（十二烷基硫酸钠变性）中能与肌营养不良蛋白和辅肌动蛋白结合，但在人肌肉冰冻切片（天然构象）中仅与辅肌动蛋白结合。它与多克隆交叉反应抗血清不同之处在于，它能与人、小鼠和鸡的几种辅肌动蛋白肌肉同工型（平滑肌型、快肌型和慢肌型）结合，并识别肌营养不良蛋白假定的三螺旋区域中一个截然不同的部分（氨基酸1750 - 2248）。结果表明，辅肌动蛋白和肌营养不良蛋白之间的结构同源性在它们的中央螺旋区域不止出现一次，并为肌营养不良蛋白的类辅肌动蛋白中央杆状模型提供了实验支持。
