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Parallel post-source decay for increasing protein identification confidence levels from 2D gels

Wåhlander, Åsa LU ; Arrigoni, Giorgio LU ; Snel, Martin; Hellman, Ulf and James, Peter LU (2008) In Proteomics 8(9). p.1771-1779
Abstract
Peptide mass fingerprinting (PMF) has over the years become one of the most commonly used tools for high-throughput analysis and identification of proteins. This method is applicable when relatively simple samples have to be analysed and it is commonly used for analysing proteins previously separated by 2-DE. The most common type of instrument used for this approach is the MALDI-TOF that has proved to be particularly suitable for the PMF analysis because of its characteristics of speed, robustness, sensitivity and automation. We have used a MALDI-TOF equipped with a novel parallel PSD capability (MALDI micro MX), to perform the analysis of two sets of different biological samples isolated by 2-DE. By using a method that integrates the data... (More)
Peptide mass fingerprinting (PMF) has over the years become one of the most commonly used tools for high-throughput analysis and identification of proteins. This method is applicable when relatively simple samples have to be analysed and it is commonly used for analysing proteins previously separated by 2-DE. The most common type of instrument used for this approach is the MALDI-TOF that has proved to be particularly suitable for the PMF analysis because of its characteristics of speed, robustness, sensitivity and automation. We have used a MALDI-TOF equipped with a novel parallel PSD capability (MALDI micro MX), to perform the analysis of two sets of different biological samples isolated by 2-DE. By using a method that integrates the data obtained by PMF analysis with the PSD data obtained in the same experiment, we show that the new multiplexed PSD solution increases the protein identification rate compared to the normal PMF approach. We also investigated the use of a charge-directed fragmentation modification reagent to improve the identification rate and confidence levels. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Proteomics
volume
8
issue
9
pages
1771 - 1779
publisher
John Wiley & Sons
external identifiers
  • wos:000255720600007
  • pmid:18442167
  • scopus:43549112305
ISSN
1615-9861
DOI
10.1002/pmic.200700894
language
English
LU publication?
yes
id
8cc0df2b-895f-486e-bf4a-8d17f4865a0d (old id 1059337)
date added to LUP
2008-04-17 15:34:56
date last changed
2017-01-01 05:13:16
@article{8cc0df2b-895f-486e-bf4a-8d17f4865a0d,
  abstract     = {Peptide mass fingerprinting (PMF) has over the years become one of the most commonly used tools for high-throughput analysis and identification of proteins. This method is applicable when relatively simple samples have to be analysed and it is commonly used for analysing proteins previously separated by 2-DE. The most common type of instrument used for this approach is the MALDI-TOF that has proved to be particularly suitable for the PMF analysis because of its characteristics of speed, robustness, sensitivity and automation. We have used a MALDI-TOF equipped with a novel parallel PSD capability (MALDI micro MX), to perform the analysis of two sets of different biological samples isolated by 2-DE. By using a method that integrates the data obtained by PMF analysis with the PSD data obtained in the same experiment, we show that the new multiplexed PSD solution increases the protein identification rate compared to the normal PMF approach. We also investigated the use of a charge-directed fragmentation modification reagent to improve the identification rate and confidence levels.},
  author       = {Wåhlander, Åsa and Arrigoni, Giorgio and Snel, Martin and Hellman, Ulf and James, Peter},
  issn         = {1615-9861},
  language     = {eng},
  number       = {9},
  pages        = {1771--1779},
  publisher    = {John Wiley & Sons},
  series       = {Proteomics},
  title        = {Parallel post-source decay for increasing protein identification confidence levels from 2D gels},
  url          = {http://dx.doi.org/10.1002/pmic.200700894},
  volume       = {8},
  year         = {2008},
}