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Complete amino acid sequence of copper-zinc superoxide dismutase from Drosophila melanogaster

  • Author(s): Lee, YM
  • Friedman, DJ
  • Ayala, FJ
  • et al.
Abstract

The complete amino acid sequence of the Drosophila melanogaster Cu,Zn Superoxide dismutase subunit has been determined by automated Edman degradation. Sequence analyses were performed on the intact S-carboxymethylated protein, two fragments derived from CNBr cleavage, and three peptides recovered from mouse submaxillary protease digestion of the reduced and S-carboxymethylated enzyme. The peptides were aligned by characterizing peptides yielded by trypsin and Staphylococcus aureus V8 protease. All the peptides studied were purified exclusively by reverse-phase columns of HPLC and were analyzed with an improved liquid-phase sequencer. A molecular weight of 15,750 (subunit) was calculated from the 151 residues sequenced. The amino acid sequence of the Drosophila Superoxide dismutase subunit is compared with that of four other eucaryotes: man, horse, cow, and yeast. Comparison of the five primary structures reveals very different rates of evolution at different times. Copper-zinc superoxide dismutase appears to be a very erratic evolutionary clock. ValValLysAlaValCysValIleAsn{A figure is presented}AspAla LysGlyThrValPhePhe Glu{A figure is presented}GluSerSerGlyThrProValLysVal{A figure is presented} GlyGluValCysGlyLeu AlaLysGly{A figure is presented}HisGlyPheHisValHisGluPhe Gly{A figure is presented}AsnThrAsnGly CysMetSerSerGly{A figure is presented}HisPheAsnProTyrGly LysGluHis{A figure is presented}AlaPro ValAspGluAsnArgHisLeu{A figure is presented}AspLeuGlyAsn IleGluAlaThrGly{A figure is presented} CysProThrLysValAsnIleThrAsp{A figure is presented}LysIleThr LeuPheGlyAlaAsp Ser{A figure is presented}IleGlyArgThrValValValHisAla {A figure is presented}AlaAspAspLeuGlyGln GlyGlyHis{A figure is presented}LeuSerLysSerThrGlyAsnAla Gly{A figure is presented}ArgIleGlyCys GlyValIleGlyIle{A figure is presented}LyS. © 1985.

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