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Titolo:
Large-gel two-dimensional electrophoresis-matrix assisted laser desorption/ionization-time of flight-mass spectrometry: An analytical challenge for studying complex protein mixtures
Autore:
Nordhoff, E; Egelhofer, V; Giavalisco, P; Eickhoff, H; Horn, M; Przewieslik, T; Theiss, D; Schneider, U; Lehrach, H; Gobom, J;
Indirizzi:
Max Planck Inst Mol Genet, Dept Lehrach, D-14195 Berlin, Germany Max Planck Inst Mol Genet Berlin Germany D-14195 D-14195 Berlin, Germany
Titolo Testata:
ELECTROPHORESIS
fascicolo: 14, volume: 22, anno: 2001,
pagine: 2844 - 2855
SICI:
0173-0835(200108)22:14<2844:LTEALD>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-FEMTOMOLE LEVEL; SEQUENCE DATABASES; POLYACRYLAMIDE GELS; IDENTIFICATION; PEPTIDE; MALDI; MS; SPECTRA; MAPS;
Keywords:
proteomics; two-dimensional electrophoresis; matrix assistet laser desorption/ionization-mass; spectrometry; peptide mapping;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Nordhoff, E Max Planck Inst Mol Genet, Dept Lehrach, Ihnestr 73, D-14195 Berlin, Germany Max Planck Inst Mol Genet Ihnestr 73 Berlin Germany D-14195y
Citazione:
E. Nordhoff et al., "Large-gel two-dimensional electrophoresis-matrix assisted laser desorption/ionization-time of flight-mass spectrometry: An analytical challenge for studying complex protein mixtures", ELECTROPHOR, 22(14), 2001, pp. 2844-2855

Abstract

The large-gel two-dimensional electrophoresis (2-DE) technique, developed by Klose and co-workers over the past 25 years, provides the resolving power necessary to separate crude proteome extracts of higher eukaryotes. Matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF-MS) provides the sample throughput necessary to identify thousands of different protein species in an adequate time period. Spot excision, in situ proteolysis, and extraction of the cleavage products from the gel matrix, peptide purification and concentration as well as the mass spectrometric sample preparation are the crucial steps that interface the two analytical techniques. Today, these routines and not the mass spectrometric instrumentation determine how many protein digests can be analyzed per day per instrument. The present paper focuses on this analytical interface and reports on an integrated protocol and technology developed in our laboratory. Automated identification of proteins in sequence databases by mass spectrometricpeptide mapping requires a powerful search engine that makes full use of the information contained in the experimental data, and scores the search results accordingly. This challenge is heading a second part of the paper.

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Documento generato il 29/10/20 alle ore 20:42:01