Evolutionary conservation of the dystrophin central rod domain.
Dystrophin cDNA fragments encoding the C-terminal repeats of the central rod region have been expressed as fusion proteins. The polyclonal antisera raised to the purified fusion proteins have been characterized and neither antiserum cross-reacted with dystrophin-related protein. Antisera detected dystrophin with molecular mass close to that of the human in all terrestrial vertebrates and amphibia studied. Experiments with antisera to the N-terminal region of the dystrophin rod confirmed that epitopes to the rod region were conserved during this evolutionary period and the length of this domain remained unaltered.[1]References
- Evolutionary conservation of the dystrophin central rod domain. Sherratt, T.G., Vulliamy, T., Strong, P.N. Biochem. J. (1992) [Pubmed]
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