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(NOS). There are three major isoforms of NOS: neural, inducible, and endothelial. Skeletal muscle expresses all three isoforms; however, the neural form, nNOS, is thought to be the predominant isoform (Kaminski and Andrade 2001). These enzymes utilize arginine as a substrate and catalyze the following reaction: L-arginine+NADPH+O2 forming L-citrulline+ NO+NADPH+. NO is important in biological systems, particularly because of its role as a second messenger. However, while NO rapidly diffuses through tissues, NO itself is a relatively short-lived species. It does have the ability to combine with other biomolecules that also have physiological importance. One example of this is its ability to combine with superoxide to form the highly oxidizing molecule peroxynitrite. Proteins are important biological targets of peroxynitrite, particularly proteins containing cysteine, motioning, and/or tryptophan (Radi et al. 2000). Several enzymes are known to be inactivated by peroxynitrite. Among these is the sarcoplasmic reticulum Ca2+-ATPase (Klebl et al. 1998). One indirect effect of NO is S-nitrosylation. In most cases, Snitrosylation events involve amines and thiols. Nitric oxide can interact with cysteines to form nitrosothiols that can alter the activity of the protein. Because of this, it has been suggested that S-nitrosylation may function as a post-translational modi cation much like phosphorylation (Jaffrey et al. 2001). Some proteins, such as the ryanodine receptor and the cysteine protease caspase3, have been shown to be endogenously nitrosylated, further supporting the suggestion that formation of nitrosothiols may be an important regulatory step (Hess et al. 2001; Hess et al. 2005). -Calpain is also a cysteine protease that could be in uenced by S-nitrosylation. Small thiol peptides like glutathione can be impacted by nitrosative stress to form compounds like S-nitrosoglutathione (GSNO). These compounds can, in turn, in uence other proteins vb.net upc-a reader VB . NET UPC-A Barcode Reader SDK - Decode & Scan UPC-A ...
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