Abstract
Background: Under conditions of oxidative stress, nitric oxide (NO) generated from arginine can combine with superoxide radicals to form peroxynitrite (PN), which is subsequently able to nitrate protein tyrosine residues to form 3-nitrotyrosine. This process is known to involve ‘uncoupling’ of NO synthase, however the precise nature of the complex relationship between NO production, and oxidative stress in vivo is still unclear. Here, we sought to investigate how PN alters NO bioavailability
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