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The microsomal lipid peroxidation system of flounder muscle was characterized as to response to temperature, cofactor requirements, inhibitors, and activators. The enzyme‐catalyzed reaction had a ratelimiting step prior to the formation of lipid hydroperoxides. The K M for NADH of the enzymic system in the presence of 0.1 mM ADP was approximately 1 μM. In the presence of Fe +3 both cysteine and ascorbate also catalyzed lipid peroxidation. While neither NADH nor ADP had an effect in the presence of ascorbate‐Fe +3 , NADH stimulated the cysteine‐Fe +3 oxidation and ADP completely inhibited it. Inhibitor studies indicated that it was a free radical reaction, an ‐SH group was involved and O 2 reduction products and singlet oxygen participated.
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McDonald et al. (1987) studied this question.
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