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

Research output: Contribution to journalArticle

7 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)395-407
Number of pages13
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume39
Issue number2
DOIs
StatePublished - Jun 15 1971

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

  • Biochemistry
  • Physiology
  • Molecular Biology

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