Brief Communications abstract
Nature Biotechnology 27, 557 - 559 (2009)
Published online: 31 May 2009 | doi:10.1038/nbt.1545
Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture
Michael T Forrester1,2, J Will Thompson3, Matthew W Foster4, Leonardo Nogueira4, M Arthur Moseley3 & Jonathan S Stamler1,4
We have modified the biotin switch assay for protein S-nitrosothiols (SNOs), using resin-assisted capture (SNO-RAC). Compared with existing methodologies, SNO-RAC requires fewer steps, detects high-mass S-nitrosylated proteins more efficiently, and facilitates identification and quantification of S-nitrosylated sites by mass spectrometry. When combined with iTRAQ labeling, SNO-RAC revealed that intracellular proteins may undergo rapid denitrosylation on a global scale. This methodology is readily adapted to analyzing diverse cysteine-based protein modifications, including S-acylation.
- Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
- Medical Scientist Training Program, Duke University Medical Center, Durham, North Carolina, USA.
- Proteomics Core Facility, Duke University Medical Center, Durham, North Carolina, USA.
- Department of Medicine, Duke University Medical Center, Durham, North Carolina, USA.
Correspondence to: Jonathan S Stamler1,4 e-mail: staml001@mc.duke.edu
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