Photo-oxidation of bovine oxymyoglobin in frozen solutions. The effect of redox active inorganic elements in muscle extracts

Sáid A. Assaf, Lyman J. Bratzler, Bruce F. Cameron, Adel A Yunis

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Abstract

1. 1. Photocatalyzed autoxidation of MbO2→MMB in frozen extracts of bovine muscle was found to obey first order kineticsas found for MbO2 of sperm-whale and horse. Formation of MMb-OH in crystallized beef MMb was studied. Its pK of ionization 8·90 is closely similar to that of sperm-whale and horse and differs from that of camel (8·53). 2. 2. Among the unbound elements examined in beef muscle extracts, iron is most responsible for photo-oxidation of MbO2. 3. 3. EDTA+iron caused further increase in oxidation. EDTA alone however, caused protection. 4. 4. Addition of ashed diffusates to beef extracts caused complete inhibition of MMb and resulted in a red pigment with absorption maxima at 580, 542 and 412 nm. 5. 5. A metmyoglobin cationic reducing agent was isolated from deproteinized horse and bovine muscle extracts by ion-exchange chromatography.

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Keywords

  • Autoxidation of oxymyoglobin
  • bovine myoglobin, metal-catalyzed oxidation
  • chelating agents, muscle reducing agents
  • color
  • cow (bos sp.)
  • fluorescent light. Freezing
  • heme proteins, sperm-whale (Physeter catadon)
  • horse (Equus caballus)
  • hydroxymetmyoglobin's spectrum
  • metmyoglobin's ionization

ASJC Scopus subject areas

  • Medicine(all)

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