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Isolation of signal transduction complexes using biotin and crosslinking methodologies. Proteomics 2007 Jul;7(14):2371-4 PMID: 17623297

Abstract

We have developed a strategy to preferentially label the N-terminal alpha-amino groups of intact proteins allowing the internal epsilon-amino groups to remain free to react with chemical crosslinking reagents. The convergence of these methodologies allows biotinylated ligands to bind to their receptors within the cell membrane followed by removal of the crosslinked complex from cell lysate. This technique allows for the isolation of protein complexes in an MS-compatible system, thus providing a tool for furthering our understanding of signal transduction.

Author List

Freed JK, Smith JR, Li P, Greene AS

Authors

Julie K. Freed MD, PhD Assistant Professor in the Anesthesiology department at Medical College of Wisconsin
Andrew S. Greene PhD Interim Vice Chair, Chief, Professor in the Biomedical Engineering department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Animals
Biotin
Cross-Linking Reagents
Protein Binding
Rats
Receptors, Tumor Necrosis Factor
Signal Transduction
Tandem Mass Spectrometry
Tumor Necrosis Factor-alpha



View this publication's entry at the Pubmed website PMID: 17623297
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