Mass spectrometric characterization of protein modification by the products of nonenzymatic oxidation of linoleic acid.

ABSTRACT: Autoxidation of linoleic acid (LA) enhanced by Fe(II)/ascorbate generates unsaturated hydroperoxides which undergo further oxidative evolution resulting in a mixture of electrophiles, including epoxyketooctadecenoic acid and dienones with intact C-18 chains as well as oxidative cleavage products such as 4-hydroxy-2(E)-nonenal (HNE), 4-oxo-2(E)-nonenal (ONE), 2(E)-octenal, 9-hydroxy-12-oxo-10(E)-dodecenoic acid, 9,12-dioxo-10(E)-dodecenoic acid, and 11-oxoundec-9(E)-enoic acid. Mass spectrometric (MALDI-TOF-MS and LC-ESI-MS/MS) studies have been performed following incubation of the model protein beta-lactoglobulin with LA, Fe(II), and ascorbate, which identified adducts of these electrophiles with three different protein nucleophiles. Deuterium labeled linoleic acid 17,17,18,18,18-d(5)-(9Z

SUBMITTER: Zhu X 

PROVIDER: S-EPMC2857685 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature