Tracking and quantification of 32P-labeled phosphopeptides in liquid chromatography matrix-assisted laser desorption/ionization mass spectrometry

Tuerk, R D; Auchli, Y; Thali, R F; Scholz, R; Wallimann, T; Brunisholz, R A; Neumann, D

doi:10.1016/j.ab.2009.04.015

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Tuerk, R. D., Auchli, Y., Thali, R. F., Scholz, R., Wallimann, T., Brunisholz, R. A., & Neumann, D. (2009). Tracking and quantification of 32P-labeled phosphopeptides in liquid chromatography matrix-assisted laser desorption/ionization mass spectrometry. Analytical Biochemistry, 390(2), 141–148. https://doi.org/10.1016/j.ab.2009.04.015

Abstract

Phosphoamino acid modifications on substrate proteins are critical components of protein kinase signaling pathways. Thus, diverse methodologies have been developed and applied to identify the sites of phosphorylated amino acids within proteins. Despite significant progress in the field, even the determination of phosphorylated residues in a given highly purified protein is not a matter of routine and can be difficult and time-consuming. Here we present a practicable approach that integrates into a liquid chromatography matrix-assisted