Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside.

@article{Yoshida1994DissociationOT,
  title={Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside.},
  author={Mitsuaki Yoshida and Akinori Suzuki and Harumi Yamamoto and Satoru Noguchi and Yoshikuni Mizuno and Eijiro Ozawa},
  journal={European journal of biochemistry},
  year={1994},
  volume={222 3},
  pages={
          1055-61
        }
}
Dystrophin is purified as a complex with several proteins from the digitonin-solubilized muscle cell membrane. Most of dystrophin-associated proteins (DAPs) are assumed to form a large oligomeric transmembranous glycoprotein complex on the sarcolemma and link dystrophin with a basement membrane protein, laminin. In the present study, we found that the purified dystrophin-DAP complex was dissociated into several groups by n-octyl-beta-D-glucoside treatment. In particular, we found that the… CONTINUE READING

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