ArticleJournal of the American Society for Mass Spectrometry2018
Direct Analysis of Proteins from Solutions with High Salt Concentration Using Laser Electrospray Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
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- Integrating protein language models and automatic biofoundry for enhanced protein evolution.Nature communications · 2025Article
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- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Rapid and flexible online desalting using Nafion-coated melamine sponge for mass spectrometry analysis.Rapid communications in mass spectrometry : RCM · 2022Article
- Clinically Viable Assay for Monitoring Uromodulin Glycosylation.Journal of the American Society for Mass Spectrometry · 2021Article
- Native Mass Spectrometry of Membrane Proteins.Analytical chemistry · 2021Review
- Atmospheric Pressure Ultraviolet Laser Desorption and Ionization from Liquid Samples for Native Mass Spectrometry.Analytical chemistry · 2019Article
- Speciation Studies of Bifunctional 3-Hydroxy-4-Pyridinone Ligands in the Presence of ZnMolecules (Basel, Switzerland) · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The detection of lysozyme, or a mixture of lysozyme, cytochrome c, and myoglobin, from solutions with varying salt concentrations (0.1 to 250 mM NaCl) is compared using laser electrospray mass spectrometry (LEMS) and electrospray ionization-mass spectrometry (ESI-MS). Protonated protein peaks were observed up to a concentration of 250 mM NaCl in the case of LEMS. In the case of ESI-MS, a protein solution with salt concentration > 0.5 mM resulted in predominantly salt-adducted features, with suppression of the protonated protein ions. The constituents in the mixture of proteins were assignable up to 250 mM NaCl for LEMS and were not assignable above a NaCl concentration of 0.5 mM for ESI. The average sodium adducts (< n >) bound to the 7+ charge state of lysozyme for LEMS measurements from salt concentrations of 2.5, 25, 50, and 100 mM NaCl are 1.71, 5.23, 5.26, and 5.11, respectively. The conventional electrospray measurements for lysozyme solution containing salt concentrations of 0.1, 1, 2, and 5 mM NaCl resulted in < n > of 2.65, 6.44, 7.57, and 8.48, respectively. LEMS displays an approximately two orders of magnitude higher salt tolerance in comparison with conventional ESI-MS. The non-equilibrium partitioning of proteins on the surface of the charged droplets is proposed as the mechanism for the high salt tolerance phenomena observed in the LEMS measurements. Graphical Abstract ᅟ.
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