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Surfactant-Induced Artifacts during Proteomic Sample Preparation
- Source :
- Analytical chemistry. 87(11)
- Publication Year :
- 2015
-
Abstract
- Bottom-up proteomics is a powerful tool for characterization of protein post-translational modifications (PTMs), where PTMs are identified at the peptide level by mass spectrometry (MS) following protein digestion. However, enzymatic digestion is associated with additional sample processing steps that may potentially introduce artifactual modifications. Here, during an MS study of the PTMs of the regulator of G-protein signaling 4, we discovered that the use of ProteaseMAX, which is an acid-labile surfactant commonly used to improve protein solubilization and digestion efficiency, can lead to in vitro modifications on cysteine residues. These hydrophobic modifications resemble S-palmitoylation and hydroxyfarnesylation, thus discouraging the use of ProteaseMAX in studies of lipid modifications of proteins. Furthermore, since they target the cysteine thiol group, the presence of these artifacts will inevitably lead to inaccuracies in quantitative analysis of cysteine modifications.
- Subjects :
- chemistry.chemical_classification
Proteomics
Molecular Structure
Protein digestion
Proteins
Peptide
In vitro
Article
Analytical Chemistry
Matrix-assisted laser desorption/ionization
Surface-Active Agents
Pulmonary surfactant
Biochemistry
chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Artifacts
Quantitative analysis (chemistry)
Cysteine
Subjects
Details
- ISSN :
- 15206882
- Volume :
- 87
- Issue :
- 11
- Database :
- OpenAIRE
- Journal :
- Analytical chemistry
- Accession number :
- edsair.doi.dedup.....c0a789fb27e3d9f9e910faf13aadbba2