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OXIDATION OF MYOGLOBIN IN VITRO MEDIATED BY LIPID OXIDATION IN MICROSOMAL FRACTIONS OF MUSCLE
Author(s) -
LIN TZONGSHIN,
HULTIN H. O.
Publication year - 1977
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.1365-2621.1977.tb01236.x
Subject(s) - myoglobin , metmyoglobin , microsome , lipid peroxidation , chemistry , biochemistry , linolenate , incubation , glutathione , pigment , peroxidase , microsoma , glutathione peroxidase , in vitro , antioxidant , hemin , enzyme , chromatography , organic chemistry , heme , fatty acid
Enzymic lipid peroxidation of a microsomal fraction prepared from chicken leg muscle led to the oxidation of oxymyoglobin to metmyoglobin when the former was incubated in vitro with the microsomal peroxidation system. Similar oxidation of pigment was observed in the presence of linolenate hydroperoxide. On prolonged incubation of myoglobin with the peroxidizing microsomal fraction, some destruction of the pigment occurred. Incubation with either BHA or a mixture of glutathione and glutathione peroxidase inhibited much of the pigment oxidation.