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Antioxidant Activity of Ceruloplasmin in Muscle Membrane and in Situ Lipid Peroxidation
Year:
1988
Authors :
Doll, Linda
;
.
Harel, Stella
;
.
Kanner, Joseph
;
.
Sofer, Frida
;
.
Volume :
36
Co-Authors:
Kanner, J., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Sofer, F., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Harel, S., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Doll, L., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Facilitators :
From page:
415
To page:
417
(
Total pages:
3
)
Abstract:
Ceruloplasmin acts as ferroxidase, catalyzing the oxidation of ferrous ions to the ferric state and reducing oxygen to water. Membranal lipid peroxidation initiated by an enzymic ADP-iron or by nonenzymic iron redox cycle systems was inhibited by ceruloplasmin. However, membranal lipid peroxidation initiated by H2O2-activated MetMb is not inhibited by ceruloplasmin. In the presence of iron ascorbate, ceruloplasmin inhibited lipid peroxidation initiated by H2O2-activated MetMb at a concentration one-tenth of that which inhibits iron ascorbate membrane lipid peroxidation. This synergistic effect seems to be derived from the possible hydroperoxidase activity of MetMb in the presence of ascorbic acid and ceruloplasmin. In situ minced turkey muscle lipid peroxidation was inhibited by ceruloplasmin, which indicates that most of this peroxidation is catalyzed by free iron ions. © 1988, American Chemical Society. All rights reserved.
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DOI :
10.1021/jf00081a003
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28308
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:38
Scientific Publication
Antioxidant Activity of Ceruloplasmin in Muscle Membrane and in Situ Lipid Peroxidation
36
Kanner, J., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Sofer, F., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Harel, S., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Doll, L., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Antioxidant Activity of Ceruloplasmin in Muscle Membrane and in Situ Lipid Peroxidation
Ceruloplasmin acts as ferroxidase, catalyzing the oxidation of ferrous ions to the ferric state and reducing oxygen to water. Membranal lipid peroxidation initiated by an enzymic ADP-iron or by nonenzymic iron redox cycle systems was inhibited by ceruloplasmin. However, membranal lipid peroxidation initiated by H2O2-activated MetMb is not inhibited by ceruloplasmin. In the presence of iron ascorbate, ceruloplasmin inhibited lipid peroxidation initiated by H2O2-activated MetMb at a concentration one-tenth of that which inhibits iron ascorbate membrane lipid peroxidation. This synergistic effect seems to be derived from the possible hydroperoxidase activity of MetMb in the presence of ascorbic acid and ceruloplasmin. In situ minced turkey muscle lipid peroxidation was inhibited by ceruloplasmin, which indicates that most of this peroxidation is catalyzed by free iron ions. © 1988, American Chemical Society. All rights reserved.
Scientific Publication
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