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Hydrogen peroxide and hematin in microsomal lipid peroxidation
Journal of Inorganic Biochemistry
|October 1, 1981
Summary
Rat liver microsomes produce malondialdehyde (MDA) during lipid peroxidation. Catalase is essential for MDA formation, as it removes hydrogen peroxide (H2O2) that would otherwise inhibit the process.
Area of Science:
- Biochemistry
- Cell Biology
Background:
- Lipid peroxidation is a process that damages cell membranes.
- Malondialdehyde (MDA) is a marker of lipid peroxidation.
- Hydrogen peroxide (H2O2) and hematin are involved in lipid peroxidation.
Purpose of the Study:
- To investigate the role of catalase in malondialdehyde (MDA) production during lipid peroxidation in rat liver microsomes.
Main Methods:
- Rat liver microsomes were incubated with H2O2 and hematin.
- Malondialdehyde (MDA) production was measured.
- The effect of histidine and catalase on MDA production was assessed.
Main Results:
- Lipid peroxidation produced MDA in rat liver microsomes with H2O2 and hematin.
- Catalase was necessary for MDA formation.
- Histidine inhibited MDA production by 55%.
Conclusions:
- Hydrogen peroxide (H2O2) initiates lipid peroxidation but inhibits MDA formation by binding to the hematin complex.
- Catalase is crucial for removing H2O2, thereby enabling the decomposition of lipid hydroperoxides into MDA.