The sequence of chick alpha-actinin reveals homologies to spectrin and calmodulin.

@article{Baron1987TheSO,
  title={The sequence of chick alpha-actinin reveals homologies to spectrin and calmodulin.},
  author={Michael D Baron and Matthew D. Davison and Patricia Jones and David R. Critchley},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 36},
  pages={
          17623-9
        }
}
We have sequenced a cDNA, isolated from a chick embryo fibroblast lambda gt11 library, that encodes all 887 amino acids of alpha-actinin. Sequence from 10 different peptides from chick smooth muscle alpha-actinin was found to match that derived from the cDNA. The deduced protein sequence can be divided into three distinct domains: (a) the N-terminal 240 amino acid contains a highly conserved region (compared with Dictyostelium alpha-actinin) which probably represents the actin-binding domain… CONTINUE READING

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