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Title: Singlet oxygen in copper-catalyzed lipid peroxidation in erythrocyte membranes

Journal Article · · Lipids; (United States)
DOI:https://doi.org/10.1007/BF02534455· OSTI ID:6743149

Lipid hydroperoxide was generated in human erythrocyte membranes by irradiation with near ultraviolet (UV) light in the presence of a photosensitizer, hematoporphyrin, but no production of 2-thiobarbituric acid-reactive materials (malonaldehyde and its precursors) was detected. Incubation of the irradiated membranes with CuSO4 led to increased levels of hydroperoxide and formation of malonaldehyde. Hydroperoxides were essential for initiating the Cu(II)-catalyzed peroxidation as no significant activity was observed with nonirradiated membranes and Cu(II) unless an organic peroxide, either t-butyl hydroperoxide or cumene hydroperoxide, was added. Catalytic activity was also found with Fe(II), but not with other metal ions tested. The peroxidation catalyzed with Cu(II) was partially inhibited by several singlet oxygen quenchers but was not affected by superoxide dismutase, catalase or OH radical scavengers. The possible involvement of singlet oxygen in the Cu(II)-catalyzed peroxidation reaction was further supported by a 3-fold enhancement of malonaldehyde production in D/sub 2/O.

Research Organization:
Department of Biochemistry, State University of New York Downstate Medical Center, Brooklyn, NY
OSTI ID:
6743149
Journal Information:
Lipids; (United States), Vol. 19:4
Country of Publication:
United States
Language:
English

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