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Iwase, H. et al.

Iwase, Sakurada, Hatanaka, Kobayashi, Takatori,

Effect of cytochrome c on the linoleic acid-degrading activity of porcine leukocyte 12-lipoxygenase.

Hemoproteins are known to have quasilipoxygenase activity that converts linoleic acid ( LA) to its hydroperoxides. However, it is not still clear whether, like lipoxygenases, hemoproteins can produce LA hydroperoxides when the LA is part of a mixture containing many different saturated and unsaturated fatty acids. In this study, we found that such hemoprotein as cytochrome c (Cyt c) did not produce LA hydroperoxides from the phospholipase A(2) (PL-A(2)) hydrolysis products of egg yolk phosphatidylcholine (PC). We also found that traces of hydroperoxides and a high concentration of the target unsaturated fatty acid ( LA) needs to be present in a fatty acid mixture before the quasi-lipoxygenase activity of Cyt c becomes apparent. We also attempted to elucidate how Cyt c interact with porcine leukocyte 12-lipoxygenase (12-LOX). Hemoproteins are known to possess pseudo-lipohydroperoxidase activity, and can remove the hydroperoxides of unsaturated fatty acids from a reaction mixture. However, we found that Cyt c catalyzed the reaction by which hydroperoxides degrade LA, and thus enhanced the LA-degrading activity of 12-LOX. This hemoprotein-induced promotion of the ability of 12-LOX to degrade LA was observed even when the reaction mixture contained many different saturated and unsaturated fatty acids.[1]

References

Effect of cytochrome c on the linoleic acid-degrading activity of porcine leukocyte 12-lipoxygenase. Iwase, H., Sakurada, K., Hatanaka, K., Kobayashi, M., Takatori, T. Free Radic. Biol. Med. (2000) [Pubmed]

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