Acetonitrile-assisted enzymatic digestion can facilitate the bottom-up identification of proteins of cancer origin
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
30660590
DOI
10.1016/j.ab.2019.01.004
PII: S0003-2697(18)30913-8
Knihovny.cz E-zdroje
- Klíčová slova
- Acetonitrile, Breast cancer, Digestion, Improvement, Protein,
- MeSH
- acetonitrily chemie MeSH
- lidé MeSH
- nádorové buněčné linie MeSH
- nádorové proteiny analýza izolace a purifikace metabolismus MeSH
- nádory metabolismus patologie MeSH
- peptidy analýza MeSH
- proteomika metody MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
- trypsin metabolismus MeSH
- vysokoúčinná kapalinová chromatografie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- acetonitrile MeSH Prohlížeč
- acetonitrily MeSH
- nádorové proteiny MeSH
- peptidy 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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