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The online- only data supplement is av... (1308).
| Content Provider | CiteSeerX |
|---|---|
| Abstract | S- nitrosylation (SNO) is a reversible, thiol- based modifica-tion that can modulate the activity of myocardial proteins, including those involved with Ca2+-handling and mitochon-drial energetics.1–4 Additionally, we and others demonstrated that SNO can protect against cysteine oxidation.4,5 This is im-portant in the setting of ischemia–reperfusion (IR) injury, in which the burst of reactive oxygen species generated at the onset of reperfusion can lead to protein oxidation and degra-dation. Myocardial ischemic preconditioning (IPC) has been shown to increase protein SNO,2,4 and thus protection from oxidation is expected to be proportionate to the percentage of protein SNO (ie, SNO occupancy). Therefore, it is important to develop a method to determine SNO occupancy. In This Issue, see p 1249 Editorial, see p 1253 Cysteine- reactive tandem mass tags (cysTMT) confer the |
| File Format | |
| Publisher Date | 1308-01-01 |
| Access Restriction | Open |
| Content Type | Text |
