Inhibition of heme-promoted enzymatic lipid peroxidation by desferrioxamine and EDTA.

Abstract:

:Oxyhemoglobin, methemoglobin and hematin were found to catalyze xanthine-oxidase-induced peroxidation of phospholipid liposomes, while oxy- and metmyoglobin were inactive in this respect. The peroxidation was inhibited by desferrioxamine and by EDTA. Peroxidation catalyzed by 0.4 microM oxyhemoglobin was decreased by 50% by approximately 2 microM desferrioxamine or 20 microM EDTA and completely inhibited by 10 microM desferrioxamine or 100 microM EDTA. Inhibition of hemoglobin-catalyzed peroxidation was not accompanied by any changes in the absorbance spectra of hemoglobin, indicating that the heme iron was not withdrawn by the inhibitor. Inhibition of hematin-catalyzed peroxidation by desferrioxamine may have been due to iron chelation and removal, as judged from changes in absorbance spectra. The peroxidation was apparently not dependent on hydrogen peroxide since catalase did not inhibit peroxidation but on the contrary promoted it in some cases.

journal_name

Ups J Med Sci

authors

Carlin G,Djursäter R,Arfors KE

doi

10.3109/03009738809178547

subject

Has Abstract

pub_date

1988-01-01 00:00:00

pages

215-23

issue

3

eissn

0300-9734

issn

2000-1967

journal_volume

93

pub_type

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