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Updated: Apr 17, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Mapping native disulfide bonds at a proteome scale.

Shan Lu¹, Sheng-Bo Fan², Bing Yang³

¹1] College of Life Science, Beijing Normal University, Beijing, China. [2] National Institute of Biological Sciences, Beijing, China.

|February 10, 2015

Summary

This summary is machine-generated.

We developed a new mass spectrometry method to precisely identify disulfide bonds in proteins. This technique mapped numerous disulfide bonds in bacteria and human cells, revealing their regulatory roles.

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Area of Science:

Biochemistry
Proteomics
Mass Spectrometry

Background:

Disulfide bonds are crucial for protein structure and function.
Identifying disulfide bonds is challenging but important for understanding cellular processes.

Purpose of the Study:

To develop a high-throughput mass spectrometry method for precise disulfide-linked peptide identification.
To map disulfide bonds in various biological systems and discover novel regulatory disulfide bonds.

Main Methods:

Developed pLink-SS, a high-throughput mass spectrometry method.
Applied pLink-SS to map disulfide bonds in a monoclonal antibody, standard proteins, Escherichia coli, and human endothelial cell-secreted proteins.

Main Results:

Precisely identified disulfide-linked peptides using pLink-SS.
Mapped all native disulfide bonds in a monoclonal antibody and ten standard proteins.
Identified 199 disulfide bonds in Escherichia coli and 568 in human endothelial cell-secreted proteins.
Discovered regulatory disulfide bonds involving catalytic or metal-binding cysteine residues.

Conclusions:

pLink-SS is an effective tool for high-throughput disulfide bond identification.
Disulfide bonds play significant regulatory roles in diverse proteomes.
The method facilitates deeper understanding of protein structure-function relationships and cellular regulation.