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

doi:10.1016/0305-0491(71)90184-2

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

Medicine

Research output: Contribution to journal › Article › peer-review

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 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	https://doi.org/10.1016/0305-0491(71)90184-2
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

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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 › peer-review

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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.",

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",

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AU - Yunis, Adel A.

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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

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KW - chelating agents, muscle reducing agents

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KW - fluorescent light. Freezing

KW - heme proteins, sperm-whale (Physeter catadon)

KW - horse (Equus caballus)

KW - hydroxymetmyoglobin's spectrum

KW - metmyoglobin's ionization

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