- P-ISSN 2233-4203
- E-ISSN 2093-8950
- P-ISSN2233-4203
- E-ISSN2093-8950
- ESCI, SCOPUS, KCI
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Enrichment Strategies for Identification and Characterization of Phosphoproteome
Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2015, v.6 no.2, pp.31-37
https://doi.org/10.5478/MSL.2015.6.2.31
(Kyung Hee University)
(Korea Research Institute of Standards and Science)
(Kyung Hee University)
(Korea Research Institute of Standards and Science)
(Kyung Hee University)
Lee,
S. Y., Kang,
D., &
Hong,
J.
(2015). . , 6(2), 31-37, https://doi.org/10.5478/MSL.2015.6.2.31
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Abstract
Phosphorylation upon protein is well known to a key regulator that implicates in modulating many cellular processes like growth, migration, and differentiation. Up to date, grafting of multidimensional separation techniques onto advanced mass spectrometry (MS) has emerged as a promising tool for figuring out the biological functions of phosphorylation in a cell. However, advanced MS-based phosphoproteomics is still challenging, due to its intrinsic issues, i.e., low stoichiometry, less susceptibility in positive ion mode, and low abundance in biological sample. To overcome these bottlenecks, diverse techniques (e.g., SCX, HILIC, ERLIC, IMAC, TiO2, etc.) are continuously developed for on-/off-line enrichment of phosphorylated protein (or peptide) from biological samples, thereby helping qualitative/quantitative determination of phosphorylated protein and its phosphorylated sites. In this review, we introduce to the overall views of enrichment tools that are universally used to selectively isolate targeted phosphorylated protein (or peptide) from ordinary ones before MS-based phospoproteomic analysis.
- keywords
- phosphoproteomics, fractionation, enrichment, nLC-ESI-MS/MS
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- 투고일Received
- 2015-05-11
- 수정일Revised
- 2015-06-17
- 게재확정일Accepted
- 2015-06-17
- 출판일Published
- 2015-06-01
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