Impact of Phosphorylation on the Mass Spectrometry Quantification of Intact Phosphoproteins.

ABSTRACT: Protein phosphorylation is a ubiquitous and critical post-translational modification (PTM) involved in numerous cellular processes. Mass spectrometry (MS)-based proteomics has emerged as the preferred technology for protein identification, characterization, and quantification. Whereas ionization/detection efficiency of peptides in electrospray ionization (ESI)-MS are markedly influenced by the presence of phosphorylation, the physicochemical properties of intact proteins are assumed not to vary significantly due to the relatively smaller modification on large intact proteins. Thus, the ionization/detection efficiency of intact phosphoprotein is hypothesized not to alter appreciably for subsequent MS quantification. However, this hypothesis has never been rigorously tested. Herein, we syste

SUBMITTER: Wu Z 

PROVIDER: S-EPMC6138620 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature