analysis of protein phosphorylation by mass spectrometry

仪器资料 · 发表于 2018-12-2 08:53:20

analysis of protein phosphorylation by mass spectrometry
The reversible phosphorylation of proteins is recognized as an essential post-translational modiWcation regulating cell signaling
and ultimately function of biological systems. Detection of phosphopeptides and localization of phosphorylation sites remains quite
a challenge, even if the protein is puriWed to near homogeneity. Mass spectrometry has become a vital technique that is routinely utilized
for the identiWcation of proteins from whole cell lysates. Nonetheless, due to the minimal amount of phosphorylation found on
proteins, enrichment steps for isolating phosphopeptides from complex mixtures have been the focus of many research groups worldwide.
In this review, we describe some current methods for the enrichment of phosphopeptides that are compatible with mass spectrometry
for assignment of phosphorylation sites. Phosphorylation modiWcations on proteins and peptides are either directly isolated
by solid-phase approaches or chemically modiWed for selective isolation and/or improved characterization by mass spectrometry.
These strategies hold the potential for rapid and sensitive proWling of phosphoproteins from a variety of sources and cellular
conditions

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