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Decreased protein nitration in macrophages that overexpress indoleamine 2, 3-dioxygenase

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Figure

Fig. 1. The activity of the tryptophan-degrading enzyme, indoleamine 2,3-dioxygenase  (IDO) requires (consumes) superoxide anion (O2 •- ), so that O2 •-  is unavailable to make  (1) hydrogen peroxide (H2O2), (2) peroxynitrite (ONOO - ), or (3) hydroxyl rad
Fig. 2. RAW 264.7 macrophages transfected with an IDO expression vector (clone 101)  or empty vector (Vo) were analyzed for (A, B) IDO expression and (C, D) IDO activity  (conversion of tryptophan to kynurenine)
Fig. 3. Comparable levels (p-values above each pair) of protein carbonyls in cell lysates  from RAW 264.7 macrophages that overexpress IDO (black bars) compared to cells that  do not express IDO (white bars)
Fig. 4. Cell lysates from RAW 264.7 macrophages that overexpress IDO (black bars)  have significantly lower levels (p-values above each pair) of nitrated proteins compared  to cells that do not express IDO (white bars)
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