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Capillary electrophoresis—matrix-assisted laser-desorption ionization mass spectrometry of proteins |
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| Authors: | Wolfgang Weinmann Carol E. Parker Leesa J. Deterding Damon I. Papac John Hoyes Michael Przybylski Kenneth B. Tomer |
| Affiliation: | a Faculty of Chemistry, University of Konstanz, 78434 Konstanz, Germany b National Institute of Environmental Health Sciences, Laboratory of Molecular Biophysics, P.O. Box 12233, Research Triangle Park, NC 27709, USA c VG Analytical, Floats Road, Wythenshawe, Manchester M23 9LE, UK |
| Abstract: | An “off-line” combination of capillary electrophoresis (CE) with matrix-assisted laser-desorption mass spectrometry (MALDI-MS) has been developed for the structural characterization of CE-separated peptides and proteins. Using a sheath flow interface, similar to that developed for “on-line” CE—fast atom bombardment MS and CE—electrospray MS, an efficient sample isolation procedure has been developed which is applicable to bioorganic compounds in aqueous buffer solutions. This isolation procedure, with subsequent transfer to the MALDI-MS sample target, has been successfully used for the direct analysis of CE-separated proteins of M r up to 67 000, and a mixture of apolipoprotein AII monomer and homodimer, using sample amounts of less than 1 pmol. |
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