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İron binding to microsomes and liposomes in relation to lipid peroxidation
Author(s) -
Vile Glenn F.,
Winterbourn Christine C.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80131-x
Subject(s) - lipid peroxidation , liposome , chemistry , microsome , biochemistry , chelation , membrane , biophysics , enzyme , inorganic chemistry , biology
The effects of ADP, ATP, citrate and EDTA on iron‐dependent microsomal and liposomal lipid peroxidation, and on 59 FeCl 3 binding to the lipid membranes were measured. The aim was to test if initiation of lipid peroxidation is a site‐specific mechanism requiring bound iron. In the absence of chelator, iron was bound to both membranes. EDTA and citrate removed the iron and inhibited peroxidation. ATP and ADP stimulated peroxidation, but whereas ADP allowed only half of the iron to remain bound, all was removed by ATP. Chelators, therefore, cannot be simply influencing a site‐specific mechanism. Their effects must relate to the reactivities of the different iron chelates as initiators of lipid peroxidation.