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pubmed:abstractText |
When porcine adrenocortical microsomes were treated with Fe2+, enhanced production of malondialdehyde was observed as a result of membrane lipid peroxidation. By treatment of the microsomes with Fe2+, the activity of delta 5-3 beta-hydroxysteroid dehydrogenase coupled with delta 5-delta 4 isomerase, concentration of cytochrome P-450 and the activity of the cytochrome-involving enzyme systems such as 17 alpha- and 21-hydroxylases were significantly reduced. 17 alpha-Hydroxylase activity was more effectively decreased by Fe2+ than that of 21-hydroxylase. On the other hand, activity of NADH- and NADPH-cytochrome c reductases remained unchanged or somewhat increased. Both the induction of lipid peroxidation and the decrease of the enzyme activities were prevented by alpha-tocopherol and N,N' -diphenyl-rho-phenylenediamine.
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