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  • Title: Proteomic method for identification of tyrosine-nitrated proteins.
    Author: Aulak KS, Koeck T, Crabb JW, Stuehr DJ.
    Journal: Methods Mol Biol; 2004; 279():151-65. PubMed ID: 15199243.
    Abstract:
    Biologic nitration of protein tyrosine (to form 3-nitrotyrosine) is a recently described phenomenon that is associated with many diseases. We have devised a proteomic methodology to identify these modified proteins. This utilizes protein fractionation by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE), partial transfer onto polyvinylidene difluoride (PVDF) membranes, and Western blot analysis using an antinitrotyrosine antibody to identify the proteins. Alignment of the Western blots with the partially transferred 2-D PAGE gels enables identification of immunopositive protein spots. These are then excised and trypsin digested. Proteins are then identified using either matrix-assisted laser desorption ionization-time of flight mass spectrometry or capillary liquid chromatography tandem electrospray mass spectrometry. Nonspecific crossreactivity of the antibodies is determined using reduction of protein bound 3-nitrotyrosine to 3-amino tyrosine using sodium dithionite.
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