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Updated: Apr 21, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Proteinase K improves quantitative acylation studies.

Benjamin Fränzel¹, Frank Fischer, Clemens Steegborn

¹Department of Analytical Chemistry, Biomolecular Mass Spectrometry, Institute of Chemistry and Biochemistry, Ruhr-Universität Bochum, Bochum, Germany.

|October 22, 2014

Summary

This summary is machine-generated.

This study introduces a novel proteomic method using proteinase K for improved detection and quantification of acetylated peptides in complex cell samples. The approach identified 557 unique acetylated peptides, advancing acetylome research.

Keywords:

Acetylation Digestion conditions Proteinase K Sirtuins Technology

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Last Updated: Apr 21, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

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

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Published on: February 27, 2020

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Area of Science:

Proteomics
Post-translational Modifications
Biochemistry

Background:

Protein acetylation is a crucial post-translational modification (PTM) but remains challenging to analyze comprehensively.
Existing methods for detecting acetylated proteins in complex biological samples require improvement for quantitative accuracy.

Purpose of the Study:

To develop and validate a robust proteomic strategy for the quantitative identification of acetylated peptides.
To evaluate proteinase K as a suitable protease for acetylome analysis.

Main Methods:

Optimization of protease digestion conditions using purified bovine histones.
Demonstration of proteinase K efficacy in complex HEK293 cell lysates.
Quantitative analysis using Stable Isotope Labeling by Amino acids in Cell culture (SILAC) coupled with Multidimensional Protein Identification Technology (MudPIT).

Main Results:

Proteinase K was identified as an effective protease for analyzing acetylated peptides.
The method successfully identified 557 unique acetylated peptides.
633 distinct acetylation sites were identified and quantified.

Conclusions:

The developed proteomic approach using proteinase K enables reliable quantitative analysis of protein acetylation.
This method significantly advances the capability for large-scale acetylome studies.
The findings provide a valuable tool for understanding the functional roles of protein acetylation.