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Simultaneous identification and quantification of nitrosylation sites by combination of biotin switch and ICAT labeling
- Source :
- Plant proteomics: methods and protocols, Plant proteomics: methods and protocols, 1072, Spinger Protocols, Humana Press, pp.609-620, 2014, Methods in Molecular Biology, Methods in Molecular Biology ISBN: 9781627036306
- Publication Year :
- 2014
- Publisher :
- HAL CCSD, 2014.
-
Abstract
- S-nitrosylation is a widespread modification of proteins. In plants, most information available to date regarding this modification was obtained using nitric oxide donors and concerned the proteins but not the identification of cysteine residues specifically modified in the proteins or their quantification. Here, we describe a method for the identification of endogenously nitrosylated cysteines in Arabidopsis and, simultaneously, the measurement of relative change in their abundance within binary comparisons.
- Subjects :
- biology
Nitrosylation
Quantitative proteomics
S-Nitrosylation
biology.organism_classification
Isotope-coded affinity tag
S-nitrosylation
Nitric oxide
chemistry.chemical_compound
ICAT labeling
Biochemistry
chemistry
Biotin Switch
Arabidopsis
Isotope-coded-affinity tag
[SDV.BV]Life Sciences [q-bio]/Vegetal Biology
[SDV.BV] Life Sciences [q-bio]/Vegetal Biology
Identification (biology)
protein
Cysteine
Subjects
Details
- Language :
- English
- ISBN :
- 978-1-62703-630-6
- ISBNs :
- 9781627036306
- Database :
- OpenAIRE
- Journal :
- Plant proteomics: methods and protocols, Plant proteomics: methods and protocols, 1072, Spinger Protocols, Humana Press, pp.609-620, 2014, Methods in Molecular Biology, Methods in Molecular Biology ISBN: 9781627036306
- Accession number :
- edsair.doi.dedup.....ce14808b0b5eef1e90fff5a40d2830df