Using electrospray laser desorption ionization mass spectrometry to rapidly examine the integrity of proteins stored in various solutions

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DOIResolve DOI: http://doi.org/10.1007/s00216-013-7491-z
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TypeArticle
Journal titleAnalytical and Bioanalytical Chemistry
ISSN1618-2650
Volume406
Issue2
Pages577586; # of pages: 10
SubjectConformations; Desorption; Drops; Filtration; Ionization; Liquid chromatography; Mass spectrometry; Proteins; Solvent extraction; Additional samples; Ambient conditions; Biochemical treatments; Chromatographic separations; ELDI; Laser desorption; Laser desorption ionization mass spectrometry; Native conformation; Electrospray ionization
AbstractElectrospray laser desorption ionization mass spectrometry (ELDI/MS) allows the rapid desorption and ionization of proteins from solutions under ambient conditions. In this study, we have demonstrated the use of ELDI/MS to efficiently examine the integrity of the proteins stored in various solutions before they were further used for other biochemical tests. The protein standards were prepared in the solutions containing buffers, organic salts, inorganic salts, strong acid, strong base, and organic solvents, respectively, to simulate those collected from solvent extraction, filtration, dialysis, or chromatographic separation. Other than the deposit of a drop of the sample solution on the metallic sample plate in an ELDI source, no additional sample pretreatment is needed. The sample drop was then irradiated with a pulsed laser; this led to desorption of the analyte molecules, which subsequently entered the ESI plume to undergo postionization. Because adjustment of the composition of the sample solution is unnecessary, this technique appears to be useful for rapidly evaluating the integrity of proteins after storage or prior to further biochemical treatment. In addition, when using acid-free and low-organic-solvent ESI solutions for ELDI/MS analysis, the native conformations of the proteins in solution could be detected. © Springer-Verlag Berlin Heidelberg 2013.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21272246
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Record identifiereeea4a6c-15df-4557-b3dc-293811386ed6
Record created2014-07-23
Record modified2016-05-09
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