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פותח על ידי קלירמאש פתרונות בע"מ -
Desferrioxamine as an electron donor. Inhibition of membranal lipid peroxidation initiated by h202 -activated metmyoglobin and other peroxidizing systems
Year:
1987
Source of publication :
Free Radical Research
Authors :
הראל, סטלה
;
.
קנר, יוסף
;
.
Volume :
3
Co-Authors:
Kanner, J., Dept. of Food Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, Israel
Harel, S., Dept. of Food Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, Israel
Facilitators :
From page:
309
To page:
317
(
Total pages:
9
)
Abstract:
Desferoxamine (DFO) involvement in several peroxidative systems was studied. These sytems included: a) membranal lipid peroxidation initiated by H2O2-activated metmyoglobin (or methemoglobin); b) phenol-red oxidation by activated metmyoglobin or horseradish peroxidase (HRP): c) βcarotene-linoleate couple oxidation stimulated by lipoxygenase or hemin. Desferrioxamine was found to inhibit all these systems but not ferrioxamine (FO). Phenol-red oxidation by H202-horseradish peroxidase was inhibited competitively with DFO. Kinetic studies using the spectra changes in the Soret region of metmyoglobin suggest a mechanism by which H202 reacts with the iron-heme to form an intermediate of oxy-ferryl myoglobin that subsequently reacts with DFO to return the activated compound to the resting state. These activities of DFO resemble the reaction of other electron donors. © 1987 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Note:
Related Files :
cell membrane
drug effect
horseradish peroxidase
iron
lipid peroxidation
metabolism
Phenol-red oxidation
עוד תגיות
תוכן קשור
More details
DOI :
10.3109/10715768709069798
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
22565
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:52
Scientific Publication
Desferrioxamine as an electron donor. Inhibition of membranal lipid peroxidation initiated by h202 -activated metmyoglobin and other peroxidizing systems
3
Kanner, J., Dept. of Food Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, Israel
Harel, S., Dept. of Food Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, Israel
Desferrioxamine as an electron donor. Inhibition of membranal lipid peroxidation initiated by h202 -activated metmyoglobin and other peroxidizing systems
Desferoxamine (DFO) involvement in several peroxidative systems was studied. These sytems included: a) membranal lipid peroxidation initiated by H2O2-activated metmyoglobin (or methemoglobin); b) phenol-red oxidation by activated metmyoglobin or horseradish peroxidase (HRP): c) βcarotene-linoleate couple oxidation stimulated by lipoxygenase or hemin. Desferrioxamine was found to inhibit all these systems but not ferrioxamine (FO). Phenol-red oxidation by H202-horseradish peroxidase was inhibited competitively with DFO. Kinetic studies using the spectra changes in the Soret region of metmyoglobin suggest a mechanism by which H202 reacts with the iron-heme to form an intermediate of oxy-ferryl myoglobin that subsequently reacts with DFO to return the activated compound to the resting state. These activities of DFO resemble the reaction of other electron donors. © 1987 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Scientific Publication
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