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פותח על ידי קלירמאש פתרונות בע"מ -
Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide
Year:
1988
Source of publication :
Free Radical Research
Authors :
הראל, סטלה
;
.
סלען, אורי (מנחם)
;
.
קנר, יוסף
;
.
Volume :
5
Co-Authors:
Harel, S., Agricultural Research Organization, The Volcani Center, Department of Food Scienct, Bet-Dagan, Israel
Salan, M.A., Agricultural Research Organization, The Volcani Center, Department of Food Scienct, Bet-Dagan, Israel
Kanner, J., Agricultural Research Organization, The Volcani Center, Department of Food Scienct, Bet-Dagan, Israel
Facilitators :
From page:
11
To page:
19
(
Total pages:
9
)
Abstract:
The reaction of H2O2 with resting metmyoglobin (MetMb), methaemoglobin (MetHb) and cytochrome-c (Cyt-c) was studied in the Soret and visible regions. The differences between the original and the final peak heights of the native haemproteins at 408 nm was found to be directly proportional to the loss of iron from the molecule. The release of iron from haemproteins was studied in a system generating H2O2 continuously at a low rate by an enzymic system, or by addition of large amounts of H2O2. Cytochrome-c, methaemoglobin and metmyoglobin during interaction with H2O2 at a concentration of 200 μM release 40% 20% and 3% respectively, of molecular iron after l0min. The inhibition of haem degradation and iron release by enzymatically-generated H2O2 was determined using several hydroxyl radical scavengers, reducing agents and antioxienzymes, such as superoxide dismutase, catalase and caeruloplasmin. © 1988 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Note:
Related Files :
animal cell
antioxidants
cattle
cytochrome c
free radicals
horse
iron
metabolism
myoglobin
superoxide dismutase
עוד תגיות
תוכן קשור
More details
DOI :
10.3109/10715768809068554
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
25508
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:15
Scientific Publication
Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide
5
Harel, S., Agricultural Research Organization, The Volcani Center, Department of Food Scienct, Bet-Dagan, Israel
Salan, M.A., Agricultural Research Organization, The Volcani Center, Department of Food Scienct, Bet-Dagan, Israel
Kanner, J., Agricultural Research Organization, The Volcani Center, Department of Food Scienct, Bet-Dagan, Israel
Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide
The reaction of H2O2 with resting metmyoglobin (MetMb), methaemoglobin (MetHb) and cytochrome-c (Cyt-c) was studied in the Soret and visible regions. The differences between the original and the final peak heights of the native haemproteins at 408 nm was found to be directly proportional to the loss of iron from the molecule. The release of iron from haemproteins was studied in a system generating H2O2 continuously at a low rate by an enzymic system, or by addition of large amounts of H2O2. Cytochrome-c, methaemoglobin and metmyoglobin during interaction with H2O2 at a concentration of 200 μM release 40% 20% and 3% respectively, of molecular iron after l0min. The inhibition of haem degradation and iron release by enzymatically-generated H2O2 was determined using several hydroxyl radical scavengers, reducing agents and antioxienzymes, such as superoxide dismutase, catalase and caeruloplasmin. © 1988 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Scientific Publication
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