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Disposable Emitters for On‐line Capillary Zone Electrophoresis/Nanoelectrospray Mass Spectrometry
Author(s) -
Bateman Kevin P.,
White Robert L.,
Thibault Pierre
Publication year - 1997
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19970215)11:3<307::aid-rcm850>3.0.co;2-m
Subject(s) - chemistry , chromatography , capillary electrophoresis , mass spectrometry , analytical chemistry (journal) , capillary action , tandem mass spectrometry , capillary electrophoresis–mass spectrometry , electrospray ionization , materials science , composite material
A new method for preparing disposable microsprayers, for on‐line capillary‐zone electrophoresis/electrospray mass spectrometry (CZE/ES‐MS) at sub‐microliter per minute flow rates, is described. Different means of coupling these microsprayers to the CZE columns are presented, and compared with the more traditional one‐piece capillary arrangement used for on‐line CZE/ES‐MS analysis. Enhancement of separation performance was obtained using capillaries coated with [(acryloylamino) propyl]trimethylammonium chloride reagents, an attractive alternative to other amine‐coated capillaries. The use of disposable microsprayers provided ease of operation and flexibility for on‐line CZE/ES‐MS experiments, since CZE columns can be prepared independently from the microsprayers. The application of these microsprayers to unattended CZE/ES‐MS operation for more than 8 hours was evaluated, and found to provide relative standard deviation values of 3–8% on peak areas and less than 1% on migration times. Full‐scan mass spectral acquisition was obtained for low femtomol injections of peptides. The technique was applied to the analysis of a single chain lectin from Phaseolus vulgaris , using both CZE/ES‐MS and CZE combined with tandem mass spectrometry. The mass spectra data obtained in this way provided information on the structure of glycopeptides identified in digests of the glycoprotein. © 1997 Crown Copyright Canada