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Capillary electrophoresis combined with 252 Cf plasma desorption and electrospray mass spectrometry for the structural characterization of hydrophobic polypeptides using organic solvents
Author(s) -
Weinmann Wolfgang,
Parker Carol E.,
Baumeister Kerstin,
Maier Claudia,
Tomer Kenneth B.,
Przybylski Michael
Publication year - 1994
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150150139
Subject(s) - chemistry , chromatography , capillary electrophoresis–mass spectrometry , capillary electrophoresis , mass spectrometry , electrospray , acetonitrile , aqueous solution , desorption , electrospray ionization , analytical chemistry (journal) , organic chemistry , adsorption
Capillary electrophoresis (CE) conditions have been developed for the separation of hydrophobic polypeptides, such as fatty acid‐acylated peptides, and their subsequent structural identification by 252 Cf plasma desorption (PDMS) and electrospray mass spectrometry (ESMS). Salt‐ and detergent‐free aqueous acetic acid buffers containing up to 20% 2‐propanol or 25% acetonitrile were employed for CE separations of hydrophobic peptides with (i) untreated, and (ii) 3‐aminopropyltrimethoxysilane‐derivatized fused silica capillaries. For both capillary types, electroosmotic flow rates suitable for sample isolation and transfer were determined, and CE separations of polypeptide mixtures were compared for aqueous buffers containing 2‐propanol or acetonitrile. For the mass spectrometric identification of CE‐separated peptides, a sheath flow sample isolation method was developed for subsequent transfer to PDMS. This procedure enabled the efficient isolation of peptide fractions for PDMS analysis, or alternative microanalytical techniques. Presented in part at the International Electrophoresis Forum, Munich, October 26–28, 1992.