PHYSCI 121 Chapter Notes - Chapter N/A: Dystrophin, Western Blot, Skeletal Muscle
Document Summary
The 156, 59, 50, 43, and 35 kd dystrophin-associated proteins each possess unique antigenic determinants, enrich quantitatively with dystrophin, and were localized to the skeletal muscle sarcolemma. The 156 kd dystrophinassociated glycoprotein contained terminally salivated ser/thr-linked oligosaccharides. These results demonstrate that dystrophin and its 59 kd associated protein are cytoskeletal elements that are tightly linked to a 156 kd extracellular glycoprotein by way of a complex of transmembrane proteins. The deduced amino acid sequence of dystrophin (koenig et al. , 1988) and its cellular localization suggest that dystrophin is a membrane-associated cytoskeletal protein. However, mab via4, bound very poorly to the native 158 kd dystrophin-associated glycoprotein, while. Mab ivd3, stained the reduced form of the 50 kd dystrophin-associated glycoprotein very weakly on immunoblots. These limitations, coupled with the need for specific probes to the 59 kd, 43 kd, and 35 kd dystrophin- associated proteins, compelled us to prepare polyclonal antisera specific for each component of the dystrophin-glycoprotein complex.
