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Lipid Peroxidation of Muscle Food: The Role of the Cytosolic Fraction
Year:
1991
Authors :
Harel, Stella
;
.
Kanner, Joseph
;
.
Sal'an, Ori (Menahem)
;
.
Shagalovich, Joseph
;
.
Volume :
39
Co-Authors:
Facilitators :
From page:
242
To page:
246
(
Total pages:
5
)
Abstract:
The cytosolic extract from turkey muscle tissues contained compounds that partially inhibited membrane lipid peroxidation initiated by an iron-redox cycle (ascorbic acid-ferric ions and iron-NADPH enzymatic reaction). The cytosolic extract, however, totally inhibited lipid peroxidation catalyzed by H2O2-activated metmyoglobin. The cytosolic extract was separated into low and high molecular weight fractions, and both fractions exhibited inhibitory effects on H2O2-activated myoglobin. Membrane lipid peroxidation initiated by the iron-redox cycle was inhibited partially by the high molecular weight fraction but accelerated by the low molecular weight fraction. Turkey muscle cytosol contains reducing compounds at a level equivalent to ~ 3 mg of ascorbic acid/100 g of fresh weight or at a concentration of approximately 150 μM. These reducing compounds, 80% of which contain ascorbic acid, seem to be responsible for the activation of the iron-redox cycle and for the inhibition of H2O2-activated myoglobin toward membranal lipid peroxidation. © 1991, American Chemical Society. All rights reserved.
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DOI :
10.1021/jf00002a003
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19056
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:26
Scientific Publication
Lipid Peroxidation of Muscle Food: The Role of the Cytosolic Fraction
39
Lipid Peroxidation of Muscle Food: The Role of the Cytosolic Fraction
The cytosolic extract from turkey muscle tissues contained compounds that partially inhibited membrane lipid peroxidation initiated by an iron-redox cycle (ascorbic acid-ferric ions and iron-NADPH enzymatic reaction). The cytosolic extract, however, totally inhibited lipid peroxidation catalyzed by H2O2-activated metmyoglobin. The cytosolic extract was separated into low and high molecular weight fractions, and both fractions exhibited inhibitory effects on H2O2-activated myoglobin. Membrane lipid peroxidation initiated by the iron-redox cycle was inhibited partially by the high molecular weight fraction but accelerated by the low molecular weight fraction. Turkey muscle cytosol contains reducing compounds at a level equivalent to ~ 3 mg of ascorbic acid/100 g of fresh weight or at a concentration of approximately 150 μM. These reducing compounds, 80% of which contain ascorbic acid, seem to be responsible for the activation of the iron-redox cycle and for the inhibition of H2O2-activated myoglobin toward membranal lipid peroxidation. © 1991, American Chemical Society. All rights reserved.
Scientific Publication
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