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פותח על ידי קלירמאש פתרונות בע"מ -
Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of "iron redox" cycle
Year:
1989
Source of publication :
Free Radical Research
Authors :
הראל, סטלה
;
.
קנר, יוסף
;
.
Volume :
6
Co-Authors:
Harel, S., Dept. of Food Science, A.R.O. The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Kanner, J., Dept. of Food Science, A.R.O. The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Facilitators :
From page:
1
To page:
10
(
Total pages:
10
)
Abstract:
Methionine was oxidized to ethylene by an "Iron Redox" system containing H2O2, Fe-EDTA and ascorbate. generating hydroxyl radicals or another species of similar reactivity. Oxy or met forms of haemoglobin and myoglobin were found to inhibit methionine oxidation. Methionine oxidation was elevated in the "Iron Redox" system by increasing ascorbic acid concentration. However, in the presence of metmyoglobin or methaemoglobin, the increases in ascorbic acid did not lower the haemproteins' inhibitory effects but rather increased them. The pro-oxidative or anti-oxidative activities of haemproteins in biological oxidative reactions seem to be dependent on compartmentalization and on the presence and concentrations of reducing compounds and H2O2. © 1989 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Note:
Related Files :
Animal
animal cell
cattle
free radicals
horse
Hydroxides
iron
methionine
Models, Biological
myoglobin
עוד תגיות
תוכן קשור
More details
DOI :
10.3109/10715768909073422
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
27054
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:27
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Scientific Publication
Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of "iron redox" cycle
6
Harel, S., Dept. of Food Science, A.R.O. The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Kanner, J., Dept. of Food Science, A.R.O. The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of "iron redox" cycle
Methionine was oxidized to ethylene by an "Iron Redox" system containing H2O2, Fe-EDTA and ascorbate. generating hydroxyl radicals or another species of similar reactivity. Oxy or met forms of haemoglobin and myoglobin were found to inhibit methionine oxidation. Methionine oxidation was elevated in the "Iron Redox" system by increasing ascorbic acid concentration. However, in the presence of metmyoglobin or methaemoglobin, the increases in ascorbic acid did not lower the haemproteins' inhibitory effects but rather increased them. The pro-oxidative or anti-oxidative activities of haemproteins in biological oxidative reactions seem to be dependent on compartmentalization and on the presence and concentrations of reducing compounds and H2O2. © 1989 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Scientific Publication
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