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Phosphopeptide analysis by directly coupling two-dimensional planar electrochromatography/thin-layer chromatography with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

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Title: Phosphopeptide analysis by directly coupling two-dimensional planar electrochromatography/thin-layer chromatography with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Authors: Panchagnula, Venkateswarlu1, Mikulskis, Alvydas1, Song, Linan1, Wang, Yang1, Wang, Mei1, Knubovets, Tanya1, Scrivener, Elaine2, Golenko, Eva1, Krull, Ira S.3, Schulz, Michael4, Heinz-Emil-Hauck4, Patton, Wayne F.1 wayne.patton@perkinelmer.com
Source: Journal of Chromatography A. Jun2007, Vol. 1155 Issue 1, p112-123. 12p.
Subjects: Chromatographic analysis, Peptides, Proteins, Mass spectrometry
Abstract: Abstract: A novel strategy is presented for the fractionation of complex peptide mixtures using two-dimensional planar electrochromatography/thin-layer chromatography (2D PEC/TLC). Phosphopeptides migrate more slowly in the first dimension, based upon their anionic phosphate residues, and certain predominantly acidic phosphopeptides even migrate in the opposite direction, relative to the bulk of the peptides. Phosphopeptides are further distinguished based upon hydrophilicity in the second dimension. This permits a restricted region of the plate to be directly interrogated for the presence of phosphopeptides by mass spectrometry (MS). Phosphopeptide analysis from the plates by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF)-MS and tandem MS enabled peptide sequencing and identification. [Copyright &y& Elsevier]
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Database: Engineering Source
Description
Abstract:Abstract: A novel strategy is presented for the fractionation of complex peptide mixtures using two-dimensional planar electrochromatography/thin-layer chromatography (2D PEC/TLC). Phosphopeptides migrate more slowly in the first dimension, based upon their anionic phosphate residues, and certain predominantly acidic phosphopeptides even migrate in the opposite direction, relative to the bulk of the peptides. Phosphopeptides are further distinguished based upon hydrophilicity in the second dimension. This permits a restricted region of the plate to be directly interrogated for the presence of phosphopeptides by mass spectrometry (MS). Phosphopeptide analysis from the plates by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF)-MS and tandem MS enabled peptide sequencing and identification. [Copyright &y& Elsevier]
ISSN:00219673
DOI:10.1016/j.chroma.2007.04.029