December 1, 1991Journal of Mass Spectrometry
Assessing the multimeric states of proteins: Studies using laser desorption mass spectrometry
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Discussion
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Implication
Biochemical analysis demonstrates stable detection of multimeric protein complexes using glutaraldehyde cross-linking and laser desorption mass spectrometry, indicating improved subunit analysis.
Key Points
- Develop a mass spectrometry-based method utilizing chemical cross-linking to preserve and characterize the native multimeric subunit states of proteins.
- Treated aqueous protein solutions with dilute glutaraldehyde to cross-link free amino groups and stabilize multimeric subunit interactions.
- Analyzed cross-linked proteins, including lysozyme, carbonic anhydrase, apomyoglobin, glucose 6-phosphate dehydrogenase, ovine lutropin, yeast alcohol dehydrogenase, avidin, and pyruvate kinase, using matrix-assisted laser desorption mass spectrometry.
- Glutaraldehyde cross-linking effectively prevented the dissociation of multimeric protein subunits during sample preparation and the laser desorption process.
- Successfully resolved intact dimeric and tetrameric protein complexes with molecular masses extending up to 250,000 Da.
Cite This Study
Farmer et al. (1991) studied this question.