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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
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Intact Protein Quantitation Using Pseudoisobaric Dimethyl Labeling.

Houqin Fang1, Kaijie Xiao1, Yunhui Li1

  • 1School of Chemical Science & Engineering and Shanghai Key Laboratory of Chemical Assessment and Sustainability, Tongji University , Shanghai 200092, China.

Analytical Chemistry
|July 1, 2016
PubMed
Summary
This summary is machine-generated.

We developed universal pseudoisobaric dimethyl labeling (pIDL) for accurate relative quantitation of intact proteins. This method efficiently labels all amino groups, enabling precise proteome analysis and discovery.

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Area of Science:

  • Proteomics
  • Mass Spectrometry
  • Biochemistry

Background:

  • Accurate protein quantitation is crucial for understanding biological functions and disease mechanisms.
  • Existing methods for intact protein quantitation face challenges in efficiency and comprehensiveness.

Purpose of the Study:

  • To develop a universal labeling strategy for the relative quantitation of intact proteins.
  • To establish a robust method for analyzing differentially expressed proteins at the molecular level.

Main Methods:

  • Development of universal pseudoisobaric dimethyl labeling (pIDL) targeting N-terminal and lysine residues.
  • Application of pIDL to standard proteins (myoglobin) and hepatocellular proteomes (HepG2 vs LO2).
  • Analysis using one-dimensional reversed-phase liquid chromatography-tandem mass spectrometry (RPLC-MS/MS) with customized heavy isotope databases.

Main Results:

  • Achieved a good linear quantitation dynamic range up to 50-fold for standard proteins.
  • Successfully quantified 33 proteins in hepatocellular proteome samples with relative standard deviation (RSD) ≤ 10%.
  • Demonstrated efficient "one-pot" labeling of all amino groups without pre-blocking.

Conclusions:

  • pIDL is a versatile and accurate method for relative quantitation of intact proteins.
  • The developed method can be extended to various intact proteome systems for comprehensive analysis.
  • This approach enhances the qualitative and quantitative information of protein species (proteoforms).