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 language | English (US) |
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Pages (from-to) | 395-407 |
Number of pages | 13 |
Journal | Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
Volume | 39 |
Issue number | 2 |
DOIs | |
State | Published - 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