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) |
|---|---|
| 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 |
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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)
Cite this
Photo-oxidation of bovine oxymyoglobin in frozen solutions. The effect of redox active inorganic elements in muscle extracts. / Assaf, Sáid A.; Bratzler, Lyman J.; Cameron, Bruce F.; Yunis, Adel A.
In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 39, No. 2, 15.06.1971, p. 395-407.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Photo-oxidation of bovine oxymyoglobin in frozen solutions. The effect of redox active inorganic elements in muscle extracts
AU - Assaf, Sáid A.
AU - Bratzler, Lyman J.
AU - Cameron, Bruce F.
AU - Yunis, Adel A
PY - 1971/6/15
Y1 - 1971/6/15
N2 - 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.
AB - 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.
KW - Autoxidation of oxymyoglobin
KW - bovine myoglobin, metal-catalyzed oxidation
KW - chelating agents, muscle reducing agents
KW - color
KW - cow (bos sp.)
KW - fluorescent light. Freezing
KW - heme proteins, sperm-whale (Physeter catadon)
KW - horse (Equus caballus)
KW - hydroxymetmyoglobin's spectrum
KW - metmyoglobin's ionization
UR - http://www.scopus.com/inward/record.url?scp=0015225914&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0015225914&partnerID=8YFLogxK
U2 - 10.1016/0305-0491(71)90184-2
DO - 10.1016/0305-0491(71)90184-2
M3 - Article
C2 - 5000933
AN - SCOPUS:0015225914
VL - 39
SP - 395
EP - 407
JO - Comparative biochemistry and physiology. B, Comparative biochemistry
JF - Comparative biochemistry and physiology. B, Comparative biochemistry
SN - 1096-4959
IS - 2
ER -