Free radical polymerization and lipid binding of lysozyme reacted with peroxidizing linoleic acid |
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Authors: | Jorge Funes Marcus Karel |
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Affiliation: | (1) Dept. of Nutrition and Food Science, M.I.T., Room 16-311, 02139 Cambridge, MA |
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Abstract: | Insolubilization and polymerization of proteins exposed to peroxidizing lipids may be due either to cross-linking with incorporation
of fragments of the lipid oxidation products, or to free radical transfer from lipid to protein and subsequent free radical
polymerization of protein. The second mechanism which has been proposed was inferred from measurements of electron spin resonance
signals in proteins. In this study, uniformly labeled linoleic acid, 14C(U)] LA, was reacted with lysozyme. Volatile oxidation products of LA were also used in some experiments. Incubation was
done in the absence of water. Oligomers of lysozyme, as well as the monomer, were isolated after incubation, and the 14C] label incorporated into each fraction was determined. The results show that the dominant mechanism of protein polymerization
after exposure to peroxidizing linoleic acid is the transfer of free radical from lipid to protein, and subsequent free radical
polymerization. |
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Keywords: | |
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