Acetonitrile-assisted enzymatic digestion can facilitate the bottom-up identification of proteins of cancer origin
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
30660590
DOI
10.1016/j.ab.2019.01.004
PII: S0003-2697(18)30913-8
Knihovny.cz E-resources
- Keywords
- Acetonitrile, Breast cancer, Digestion, Improvement, Protein,
- MeSH
- Acetonitriles chemistry MeSH
- Humans MeSH
- Cell Line, Tumor MeSH
- Neoplasm Proteins analysis isolation & purification metabolism MeSH
- Neoplasms metabolism pathology MeSH
- Peptides analysis MeSH
- Proteomics methods MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Trypsin metabolism MeSH
- Chromatography, High Pressure Liquid MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- acetonitrile MeSH Browser
- Acetonitriles MeSH
- Neoplasm Proteins MeSH
- Peptides MeSH
- Trypsin MeSH
The main objective of this study was to develop an effective in-gel trypsin digestion protocol using aqueous-acetonitrile solvent system to facilitate MS analysis and maximize the number of identified proteins from biological samples. The procedure, where 80% acetonitrile was present in the trypsin reaction mixture, increased the number of matched peptides, and allowed the identification of more proteins with higher coverage than the common digestion protocol. Vimentin, annexins, tubulin, actin, peptidyl-prolyl cis-trans isomerase or alpha-enolase are examples of important proteins that change during the progress cancer. These were isolated from human breast cancer cells and were used for this study.
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