Oxidation desensitizes actomyosin to magnesium pyrophosphate-induced dissociation

Zelong Liu, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


This study aimed to establish the influence of protein oxidation on the ability of magnesium pyrophosphate (PP) to dissociate actomyosin. Actomyosin isolated from pork muscle then suspended in 0.1 M NaCl at pH 6.2 was oxidatively stressed with 10 μM FeCl3/0.1 mM ascorbate/1 mM H 2O2 for 6 or 12 h at 4 °C. Protein oxidation was evidenced by the loss of myosin and actin, the concomitant formation of disulphide-cross-linked polymers, and elevated myosin ATPase activity. The intrinsic viscosity of oxidized actomyosin had a weaker response to PP-Mg 2+ than that of non-oxidized actomyosin, indicating the suppression of actomyosin dissociation. Moreover, oxidized actomyosin solutions were devoid of small particles (<10 nm) and the stressed actomyosin exhibited weaker binding of PP-Mg2+ than non-oxidized, which further suggested a reduced myosin-PP interaction and subsequent dissociation of the actomyosin complexes.

Original languageEnglish
Pages (from-to)662-668
Number of pages7
JournalFood Chemistry
Issue number2
StatePublished - 2013

Bibliographical note

Funding Information:
This research was supported by USDA AFRI Grant 2008-35503-18790 (to Y.L.X.) and an Oversea Study Fellowship from the China Scholarship Council (to Z.L.). Approved for publication as journal article number 12-07-137 by the Director of the Kentucky Agricultural Experiment Station.


  • ATPase activity
  • Actomyosin dissociation
  • Oxidation
  • Pyrophosphate

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science


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