Liposome-recruited activity of oxidized and fragmented superoxide dismutase

Le Quoc Tuan, Hiroshi Umakoshi, Toshinori Shimanouchi, Ryoichi Kuboi

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


The peptide fragment of H2O2-treated Cu,Zn-superoxide dismutase (SOD) was found to be reactivated with liposomes prepared by l-palmitoyl-2-oleoyl-.m-glycero-3-phosphocholine (POPC). The fragmentation of SOD was observed by 2 mM H2O2 treatment as well as by SOD inactivation and the loss of an α-helix in the neighborhood of its activity center. The H2O2-treated SOD, which lost its activity at different incubation times, was dramatically reactivated only by adding POPC liposomes, resulting in 1.3-2.8 times higher enzymatic activity. The ultrafiltration analysis of H2O2-treated SOD co-incubated with liposomes shows that some specific peptide fragments of the oxidized SOD can interact with POPC liposomes. A comparison of the fractions detected in reverse-phase chromatography shows that specific SOD fragments are able to contribute to the reactivation of oxidized and fragmented SOD in the presence of POPC liposomes. The liposomes can recruit the potentially active fragment of SOD among the lethally damaged SOD fragments to elucidate the antioxidative function.

Original languageEnglish
Pages (from-to)350-354
Number of pages5
Issue number2
Publication statusPublished - Jan 15 2008
Externally publishedYes

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry


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