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Journal of Lipid Research, Vol. 4, 204-207, April 1963
Copyright © 1963 by Lipid Research, Inc.

Damage to proteins by peroxidized lipids

I. D. Desai and A. L. Tappel

Department of Food Science and Technology, University of California, Davis, California

The purpose of this research was to determine the mechanism of damage to protein by the free radical intermediates formed during the peroxidation of lipids. The reaction system consisted of linolenic acid, cytochrome c, and oxygen. The addition reaction of peroxidizing linolenic acid with cytochrome c was measured using linolenic acid-C¹⁴. There was considerable damage to cytochrome c as measured by its decreased solubility. Paper chromatographic studies of the amino acids of the linolenic peroxy-cytochrome c product showed losses of amino acids that are labile to oxidation. Linkages between linolenic acid and cytochrome c were identified as either peroxy or ether by infrared spectra. Hydrolysis revealed that 70% of the linolenic acid was bound to cytochrome c through peroxy bonds, and the rest through ether or possibly carbon-to-carbon bonds. Measurements of thiobarbituric acid value and peroxide number substantiated the chemical nature of peroxidative damage to cytochrome c.

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