Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates.
Protein phosphorylation may be the most widespread and possibly most important post-translational modification (PTM). Considering such a claim, it should be no surprise that huge efforts have been made to improve methods to allow comprehensive study of cellular phosphorylation events. Nevertheless,...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2008
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| _version_ | 1797085084134670336 |
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| author | Mohammed, S Kraiczek, K Pinkse, M Lemeer, S Benschop, J Heck, A |
| author_facet | Mohammed, S Kraiczek, K Pinkse, M Lemeer, S Benschop, J Heck, A |
| author_sort | Mohammed, S |
| collection | OXFORD |
| description | Protein phosphorylation may be the most widespread and possibly most important post-translational modification (PTM). Considering such a claim, it should be no surprise that huge efforts have been made to improve methods to allow comprehensive study of cellular phosphorylation events. Nevertheless, comprehensive identification of sites of protein phosphorylation is still a challenge, best left to experienced proteomics experts. Recent advances in HPLC chip manufacturing have created an environment to allow automation of popular techniques in the bioanalytical world. One such tool that would benefit from the increased ease and confidence brought by automated 'nanoflow' analysis is phosphopeptide enrichment. To this end, we have developed a reusable HPLC nanoflow rate chip using TiO 2 particles for selective phosphopeptide enrichment. Such a design proved robust, easy to use, and was capable of consistent performance over tens of analyses including minute amounts of complex cellular lysates. |
| first_indexed | 2024-03-07T02:04:07Z |
| format | Journal article |
| id | oxford-uuid:9e604ccd-2cd8-4b4e-9b7f-a28a3e0cd2fb |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:04:07Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:9e604ccd-2cd8-4b4e-9b7f-a28a3e0cd2fb2022-03-27T00:49:40ZChip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9e604ccd-2cd8-4b4e-9b7f-a28a3e0cd2fbEnglishSymplectic Elements at Oxford2008Mohammed, SKraiczek, KPinkse, MLemeer, SBenschop, JHeck, AProtein phosphorylation may be the most widespread and possibly most important post-translational modification (PTM). Considering such a claim, it should be no surprise that huge efforts have been made to improve methods to allow comprehensive study of cellular phosphorylation events. Nevertheless, comprehensive identification of sites of protein phosphorylation is still a challenge, best left to experienced proteomics experts. Recent advances in HPLC chip manufacturing have created an environment to allow automation of popular techniques in the bioanalytical world. One such tool that would benefit from the increased ease and confidence brought by automated 'nanoflow' analysis is phosphopeptide enrichment. To this end, we have developed a reusable HPLC nanoflow rate chip using TiO 2 particles for selective phosphopeptide enrichment. Such a design proved robust, easy to use, and was capable of consistent performance over tens of analyses including minute amounts of complex cellular lysates. |
| spellingShingle | Mohammed, S Kraiczek, K Pinkse, M Lemeer, S Benschop, J Heck, A Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates. |
| title | Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates. |
| title_full | Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates. |
| title_fullStr | Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates. |
| title_full_unstemmed | Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates. |
| title_short | Chip-Based Enrichment and NanoLC-MS/MS Analysis of Phosphopeptides from Whole Lysates. |
| title_sort | chip based enrichment and nanolc ms ms analysis of phosphopeptides from whole lysates |
| work_keys_str_mv | AT mohammeds chipbasedenrichmentandnanolcmsmsanalysisofphosphopeptidesfromwholelysates AT kraiczekk chipbasedenrichmentandnanolcmsmsanalysisofphosphopeptidesfromwholelysates AT pinksem chipbasedenrichmentandnanolcmsmsanalysisofphosphopeptidesfromwholelysates AT lemeers chipbasedenrichmentandnanolcmsmsanalysisofphosphopeptidesfromwholelysates AT benschopj chipbasedenrichmentandnanolcmsmsanalysisofphosphopeptidesfromwholelysates AT hecka chipbasedenrichmentandnanolcmsmsanalysisofphosphopeptidesfromwholelysates |