אסיף מאגר המחקר החקלאי

Desferrioxamine as an electron donor. Inhibition of membranal lipid peroxidation initiated by h202 -activated metmyoglobin and other peroxidizing systems

Year:

1987

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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

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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.

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