Article ID Journal Published Year Pages File Type
1205811 Journal of Chromatography A 2008 11 Pages PDF
Abstract

The development of an integrated chromatographic system for complete phosphoprotein analysis is described. The digestion of phosphoproteins with trypsin- or pronase-based monolithic bioreactors is carried out on-line with selective enrichment on a TiO2 trap and separation of the produced phosphopeptides by reversed-phase liquid chromatography-multiple mass spectrometry (RPLC/MSn). A detailed study on the selective extraction of peptides with different degrees of phosphorylation on TiO2 cartridges is discussed. This analytical strategy has been optimized using β-casein as a standard phosphoprotein, and then applied to the identification of phosphorylation sites in insulin-like grow factor-binding protein 1 (IGFBP-1) isolated from amniotic fluid.

Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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