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Titolo:
Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry
Autore:
Belghazi, M; Bathany, K; Hountondji, C; Grandier-Vazeille, X; Manon, S; Schmitter, JM;
Indirizzi:
Univ Bordeaux 1, UMR CNRS 5472, Lab Phys Tox Chim, F-33405 Talence, FranceUniv Bordeaux 1 Talence France F-33405 Tox Chim, F-33405 Talence, France Inst Europeen Chim Biol, Talence, France Inst Europeen Chim Biol TalenceFrance opeen Chim Biol, Talence, France Ecole Polytech, UMR CNRS 7654, Biochim Lab, Palaiseau, France Ecole Polytech Palaiseau France RS 7654, Biochim Lab, Palaiseau, France Inst Biol & Genet Cellulaire, CNRS, Bordeaux, France Inst Biol & Genet Cellulaire Bordeaux France re, CNRS, Bordeaux, France
Titolo Testata:
PROTEOMICS
fascicolo: 8, volume: 1, anno: 2001,
pagine: 946 - 954
SICI:
1615-9853(200108)1:8<946:AOPSAP>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
DESORPTION IONIZATION; SACCHAROMYCES-CEREVISIAE; MALATE-DEHYDROGENASE; 2-DIMENSIONAL GELS; SAMPLE PREPARATION; CITRATE SYNTHASE; IN-VIVO; PEPTIDE; YEAST; DATABASES;
Keywords:
matrix-assisted laser desorption/ionization spectral suppression; post-source decay; protein sequence verification; supramolecular protein complex; yeast NADH dehydrogenases; aminoacyl-tRNA synthetases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Schmitter, JM Univ Bordeaux 1, UMR CNRS 5472, Lab Phys Tox Chim, F-33405 Talence, France Univ Bordeaux 1 Talence France F-33405 405 Talence, France
Citazione:
M. Belghazi et al., "Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry", PROTEOMICS, 1(8), 2001, pp. 946-954

Abstract

In the context of proteome analysis, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) can fulfil the two tasks of primary structure verification and protein identification. As an illustration of the first of these tasks, the sequence of Eschericha colt isoleucyl-tRNA synthetase, a protein with 15 reported sequence conflicts, has been established bymeans of MALDI mass mapping. The identification of mitochondrial proteins participating in a yeast supramolecular complex exhibiting NADH dehydrogenase activity highlights the performances of MALDI-MS for the second task. The spectral suppression phenomenon occurring for complex peptide mixtures analysed by MALDI is discussed, as well as the role of post-source decay analysis for confident protein identification.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 04:00:57