Iodoacetyl Tandem Mass Tags for Cysteine Peptide Modification, Enrichment and Quantitation
نویسندگان
چکیده
منابع مشابه
Proteome profiling of s-nitrosylated synaptosomal proteins by isobaric mass tags
Background: Reversible redox-based modifications of cysteine play an essential role in physiological and pathophysiological conditions. Mass spectrometric detection of S-nitrosylated (SNO) proteins can be challenging due to low abundance of the modification and SNO bond instability. Therefore, there is a demand for highly sensitive quantitation procedures in particular when analyzing cellular c...
متن کاملQuantitative analysis of the cysteine redoxome by iodoacetyl tandem mass tags
The redox conditions that reign inside a cell have a determining effect on a number of biological processes. Reactive oxygen species (ROS) and reactive nitrogen species (RNS) are key redox players and have been linked to a number of pathologies. They have also been shown to play an important regulating role in cell signaling events. On the proteome level, thiol groups of cysteinyl side chains c...
متن کاملDesign and synthesis of visible isotope-coded affinity tags for the absolute quantification of specific proteins in complex mixtures.
Identification of proteins in complex mixtures by mass spectrometry is most useful when quantitative data is also obtained. We recently introduced isotope-coded affinity tags (ICAT reagents) for the relative quantification of proteins present in two or more biological samples. In this report, we describe a new generation of ICAT reagents that contain the following additional features: (1) a vis...
متن کاملDual Labeling Biotin Switch Assay to Reduce Bias Derived From Different Cysteine Subpopulations: A Method to Maximize S-Nitrosylation Detection.
RATIONALE S-nitrosylation (SNO), an oxidative post-translational modification of cysteine residues, responds to changes in the cardiac redox-environment. Classic biotin-switch assay and its derivatives are the most common methods used for detecting SNO. In this approach, the labile SNO group is selectively replaced with a single stable tag. To date, a variety of thiol-reactive tags have been in...
متن کاملDual quinone tagging for MALDI-TOF mass spectrometric quantitation of cysteine-containing peptide.
A dual quinone tagging strategy is designed for quantitation of cysteine-containing peptide (CCP) with MALDI-TOF mass spectrometry. The quinone compounds can rapidly and specifically bind to the thiol group of cysteine residues by a Michael addition reaction, which is used to identify both CCP and the number of cysteine residues in CCP through the direct observation of untagged and tagged produ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2012