Multiple electrophoretic variants of Cu, Zn superoxide dismutase as expression of the enzyme aging. Effects of H2O2, ascorbate and metal ions

Irene Mavelli, Maria Rosa Ciriolo, Giuseppe Rotilio

Research output: Contribution to journalArticlepeer-review

Abstract

Multiple electrophoretic bands, with RF identical to the natural molecular variants, are produced by treatment of purified Cu, Zn Superoxide dismutase with either H2O2 or ascorbate plus Fe(III) EDTA. The ascorbate reaction is also due to H2O2 since it is inhibited by catalase. However while H2O2 inactivates the enzyme, the electromorphs produced by ascorbate-Fe(III) EDTA have only slightly less activity than the native enzyme and this property parallels the natural situation. It is concluded that oxidative aging can be responsible for the multiple molecular variants of the natural enzyme, under conditions where the oxidant attack is preferentially directed to amino acid side chains outside the active site. Such conditions may occur when a metal ion coordinated to the protein surface undergoes a redox cycle with biological reductants, like ascorbate.

Original languageEnglish
Pages (from-to)677-681
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume117
Issue number3
DOIs
Publication statusPublished - Dec 28 1983

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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