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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Updated: May 17, 2026

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

Published on: May 4, 2022

Complementary workflow for global phosphoproteome analysis.

Qing-Run Li¹, Zhi-Bin Ning, Xing-Lin Yang

¹Key Laboratory of Systems Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.

Electrophoresis

|October 26, 2012

Summary

This summary is machine-generated.

This study presents a new workflow for phosphoproteome analysis using titanium dioxide enrichment and ion-exchange chromatography. This method efficiently identifies thousands of unique phosphosites from cell lysates.

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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

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Last Updated: May 17, 2026

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

Published on: May 4, 2022

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

Proteomics
Biochemistry
Analytical Chemistry

Background:

Phosphoproteome analysis is crucial for understanding cellular signaling pathways.
Existing enrichment methods face challenges in selectivity and sample capacity.
Efficient fractionation is key to comprehensive phosphopeptide identification.

Purpose of the Study:

To develop and validate a robust workflow for global phosphoproteome analysis.
To optimize titanium dioxide enrichment and ion-exchange chromatography for phosphopeptide recovery.
To enhance the depth and breadth of phosphosite identification.

Main Methods:

Combined offline titanium dioxide (TiO2) enrichment with online strong anion exchange (SAX) and strong cation exchange (SCX) fractionation.
Utilized reversed-phase liquid chromatography coupled with tandem mass spectrometry (RP-LC-MS/MS).
Optimized peptide-to-beads ratio for TiO2 enrichment to maximize selectivity and loading capacity.

Main Results:

Achieved high selectivity and sample loading capacity with offline TiO2 enrichment.
Demonstrated complementary identification of phosphopeptides across SAX, SCX, and flow-through fractions.
Successfully identified 5063 unique phosphosites from 4557 unique phosphopeptides using 4-mg HeLa cell lysate.

Conclusions:

The integrated workflow significantly enhances phosphoproteome coverage.
Offline TiO2 enrichment followed by IEC fractionation is effective for deep phosphoproteome profiling.
This approach enables the recovery of a substantial number of multiphosphopeptides.