Antinitrotyrosine Antibody

We have raised antibodies to a nitrated protein which specifically recognize the nitrotyrosine moiety. Binding of the antinitrotyrosine antibody is 

Perhaps more importantly from the standpoint of specificity, chemical reduction of the nitro group to amino totally prevents antibody binding. The inability of the antibody to recognize aminotyrosine, in spite of its structural similarity to nitrotyrosine, indicates an extremely high degree of specificity. 

No cross-reactivity has been seen with other nitro aromatics, such as nitro-phenylalanine, nitrotryptophan, or nitroguanine, nor with physiological tyrosine analogs such as phosphostyrosine, chlorotyrosine, dopamine, DOPA, dopamine, or tyramine (Ye et al., 1995). 

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Chlorination products (mainly chlorotyrosine) are measured by HPLC (Fig. 8) or gas chromatography-mass spectrometry. Also, 3-nitrotyrosine can be detected in protein hydrolysates by HPLC in combination with various detection systems, including UV and electrochemical detection (Cl7, C20, L23, L24, 04, S26), gas chromatography, gas chromatography-mass spectrometry (J2), electrospray mass spectrometry, and Western blotting or ELISA using antinitrotyrosine antibodies (H20, T2, V6). 

Using the antinitrotyrosine antibody, we and others have seen specific staining for nitrated protein in a number of diseases and conditions, including the endothelium and plaques in atherosclerotic vessels (Beckman et al.,... 

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