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Reduction of Metmyoglobin by Extracts of Bovine Liver and Cardiac Muscle
Author(s) -
FAUSTMAN C.,
CASSENS R.G.,
GREASER M.L.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb13531.x
Subject(s) - metmyoglobin , chemistry , reductase , cytochrome , biochemistry , enzyme , cytochrome c , potassium cyanide , cyanide , substrate (aquarium) , potassium ferrocyanide , myoglobin , biology , inorganic chemistry , mitochondrion , ecology
Enzymatic reduction of metmyoglobin ( in vivo ) was investigated using a partially purified metmyoglobin reductase from bovine cardiac muscle. Greater substrate reduction (P<0.05) occurred at pH 6.3 versus 7.0 or 7.3 and at 375°C compared to 22°C using either partially purified cytochrome as or potassium ferrocyanide as reaction mediators. Differences in effectiveness between potassium ferrocyanide and the cytochrome b, preparation were dependent on specific pH/temperature conditions. The cytochrome preparation alone (i.e. without metmyoglobin reductase) reduced metmyoglobin at a rate comparable to that of the reductase. At 22°C the cytochrome b=, preparation assay displayed much slower re‐oxidation than the cardiac reductase/ferro‐cyanide assay (48 vs 2 hr, respectively).