Publication Details

Category Text Publication
Reference Category Journals
DOI 10.1016/j.ymeth.2004.08.015
Title (Primary) Peptide mass fingerprinting
Author Thiede, B.; Höhenwarter, W.; Krah, A.; Mattow, J.; Schmid, M.; Schmidt, F.; Jungblut, P.R.
Source Titel Methods
Year 2005
Department PROTEOM
Volume 35
Issue 3
Page From 237
Page To 247
Language englisch
Keywords MALDI-MS; minimal protein identifier; MS-screener; peptide mass fingerprinting; proteome; proteomics
Abstract Peptide mass fingerprinting by MALDI-MS and sequencing by tandem mass spectrometry have evolved into the major methods for identification of proteins following separation by two-dimensional gel electrophoresis, SDS-PAGE or liquid chromatography. One main technological goal of proteome analyses beside high sensitivity and automation was the comprehensive analysis of proteins. Therefore, the protein species level with the essential information on co- and post-translational modifications must be achieved. The power of peptide mass fingerprinting for protein identification was described here, as exemplified by the identification of protein species with high molecular masses (spectrin alpha and beta), low molecular masses (elongation factor EF-TU fragments), splice variants (alpha A crystallin), aggregates with disulfide bridges (alkylhydroperoxide reductase), and phosphorylated proteins (heat shock protein 27). Helpful tools for these analyses were the use of the minimal protein identifier concept and the software program MS-Screener to remove mass peaks assignable to contaminants and neighbor spots. (c) 2004 Elsevier Inc. All rights reserved
Persistent UFZ Identifier
Thiede, B., Höhenwarter, W., Krah, A., Mattow, J., Schmid, M., Schmidt, F., Jungblut, P.R. (2005):
Peptide mass fingerprinting
Methods 35 (3), 237 - 247 10.1016/j.ymeth.2004.08.015