Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes.

@article{Ogawa1997StabilityOM,
  title={Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes.},
  author={Yasuhiro Ogawa and Hiroaki Kosaka and Takeo Nakanishi and Atsushi Shimizu and N Ohoi and Hisashi Shouji and Takehiko Yanagihara and Saburo Sakoda},
  journal={Biochemical and biophysical research communications},
  year={1997},
  volume={241 2},
  pages={
          251-7
        }
}
We analyzed mutant superoxide dismutase-1 (SOD-1) in erythrocytes from patients with familial amyotrophic lateral sclerosis (FALS) by using ion exchange chromatography and HPLC/electrospray ionization mass spectrometry and were able to divide mutant SOD-1 proteins into a stable form including G37R and H46R, and an unstable form including I149T and a two base pair deletion mutant. Each mutant sample showed abnormal copper peaks in different chromatographic fractions without relation to SOD-1… CONTINUE READING
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