Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins.

@article{Mitsui2002PurificationOP,
  title={Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins.},
  author={Kenichi Mitsui and Hiroshi Nakayama and Takumi Akagi and Munenori Nekooki and Kenji Ohtawa and Koji Takio and Tsutomu Hashikawa and Nobuyuki Nukina},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2002},
  volume={22 21},
  pages={9267-77}
}
Aggregates of green fluorescent protein (GFP)-fused truncated N-terminal huntingtin containing abnormally long polyglutamine tracts (150 repeats of glutamine residue) were purified from an ecdysone-inducible mutant neuro2A cell line (HD150Q-28) by using a fluorescence-activated cell sorter. To analyze the aggregate-interacting proteins, we subjected the purified aggregates to SDS-PAGE; prominent protein bands in the gel were digested with Achromobactor lysyl endopeptidase, followed by a HPLC… CONTINUE READING