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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
Published on: July 31, 2011
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Neutron-encoded protein quantification by peptide carbamylation.
Arne Ulbrich1, Anna E Merrill, Alexander S Hebert
1Department of Chemistry, University of Wisconsin, Madison, WI, 53706, USA.
Journal of the American Society for Mass Spectrometry
|November 2, 2013
Summary
We developed a new chemical tag called neutron encoding (NeuCode) for accurate proteome quantification. This method efficiently measures protein expression changes, such as in mice on different diets.
Area of Science:
- Biochemistry
- Proteomics
- Analytical Chemistry
Background:
- Accurate quantification of protein expression is crucial for understanding biological processes and disease.
- Existing duplex proteome quantification methods can be complex or expensive.
Purpose of the Study:
- To introduce and validate a novel chemical tagging strategy for duplex proteome quantification.
- To demonstrate the efficiency and accuracy of the carbamylation reaction for this purpose.
Main Methods:
- Developed a chemical tag utilizing the carbamylation reaction for neutron encoding (NeuCode).
- Applied NeuCode to quantify known ratios of tagged yeast lysates.
- Utilized NeuCode to analyze differential protein expression in mice fed control versus high-fat diets.
Main Results:
- NeuCode accurately measured quantitative ratios from tagged yeast lysates.
- Successfully quantified differential protein expression in response to dietary changes in mice.
Conclusions:
- NeuCode provides a straightforward, efficient, and inexpensive method for duplex proteome quantification.
- This technique is valuable for comparative proteomics studies, including those involving diet-induced changes in protein expression.
