Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems

Tooru Ooizumi, Youling L. Xiong

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107 Scopus citations


Biochemical changes of myosin in chicken myofibrils exposed to nonenzymatic, hydroxyl radical generation systems (HRGS) were investigated by means of cross-linking reaction, ATPase activity, salt solubility, and 40% saturated ammonium sulfate (AS) extractability. HRGS treatment of myofibrils caused cross-linking of myosin heavy chains (MHC) via disulfide bonding, an increase in Ca-ATPase activity, and a decrease in K-ATPase activity, suggesting that thiol groups of myosin including those at the active site were modified. The specific changes depended on the concentrations of H2O 2 in HRGS as well as the weight ratio of H2O2 to myofibrils. On the other hand, the decrease in salt solubility or AS extractability of myosin in HRGS-treated samples proceeded slowly when compared with the cross-linking reaction of MHC, indicating that considerable amounts of myosin biopolymers remained hydrophilic in the ionic solutions. The results demonstrated that initial cross-linking of MHC occurred inside the myosin molecule, and this was followed by progressive aggregation of myosin molecules through intermolecular cross-linking. Oxidation under the current experimental condition decreased the gel-forming ability of myofibrillar proteins, which coincided with the progress of the intra- and intermolecular cross-linking reactions as well as with ATPase activity changes.

Original languageEnglish
Pages (from-to)4303-4307
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Issue number13
StatePublished - Jun 30 2004


  • Aggregation
  • ATPase activity
  • Cross-linking
  • Myofibrils
  • Myosin
  • Oxidation
  • Thiol groups

ASJC Scopus subject areas

  • Chemistry (all)
  • Agricultural and Biological Sciences (all)


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