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.
N1 - Funding Information:
Acknowledgement--This work was supported by U.S.P.H.S. Grant No. AM-09001-06, The Michigan Agriculture Experiment Station and the Council for Tobacco Research, U.S., Grant No. 661. Financial graduate research support to S.A.A. by Michigan State University is acknowledged. Technical assistance in preparation of deproteinized extracts by Olga J. Carvajalino is greatly appreciated.
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
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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 -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
SN - 0305-0491
IS - 2
ER -