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Titolo:
Automated LC-LC-MS-MS platform using binary ion-exchange and gradient reversed-phase chromatography for improved proteomic analyses
Autore:
Davis, MT; Beierle, J; Bures, ET; McGinley, MD; Mort, J; Robinson, JH; Spahr, CS; Yu, W; Luethy, R; Patterson, SD;
Indirizzi:
Amgen Inc, Dept Biochem, Thousand Oaks, CA 91320 USA Amgen Inc Thousand Oaks CA USA 91320 Biochem, Thousand Oaks, CA 91320 USA Amgen Inc, Dept Computat Biol, Thousand Oaks, CA 91320 USA Amgen Inc Thousand Oaks CA USA 91320 at Biol, Thousand Oaks, CA 91320 USA Celeva Genom, Rockville, MD 20850 USA Celeva Genom Rockville MD USA 20850Celeva Genom, Rockville, MD 20850 USA
Titolo Testata:
JOURNAL OF CHROMATOGRAPHY B
fascicolo: 2, volume: 752, anno: 2001,
pagine: 281 - 291
SICI:
1387-2273(20010310)752:2<281:ALPUBI>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
MASS-SPECTROMETRY; LIQUID-CHROMATOGRAPHY; PROTEINS; IDENTIFICATION; PEPTIDES; DATABASE; MIXTURES; LEVEL; TAGS; GEL;
Keywords:
proteomics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Davis, MT Amgen Inc, Dept Biochem, Thousand Oaks, CA 91320 USA Amgen Inc Thousand Oaks CA USA 91320 housand Oaks, CA 91320 USA
Citazione:
M.T. Davis et al., "Automated LC-LC-MS-MS platform using binary ion-exchange and gradient reversed-phase chromatography for improved proteomic analyses", J CHROMAT B, 752(2), 2001, pp. 281-291

Abstract

A simple multidimensional liquid chromatography system utilizing an isocratic pump and a HPLC system is described for the comprehensive proteomic analysis of complex peptide digest mixtures by coupled LC-LC-MS-MS techniques. A binary ion-exchange separation was achieved through the use of a strong cation-exchange column followed by a reversed-phase column for data-dependent LC-MS-MS analysis of the unbound analytes, and following salt elution (and concomitant column reequilibration), the bound analytes. Off-line validation of the platform showed near quantitative recovery of fractionated peptides and essentially complete ion-exchange partitioning. In comparative analyses of a highly complex peptide digest mixture a >40% increase in the number of peptide and protein identifications was achieved using this multidimensional platform compared to an unfractionated control. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:35:19