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Titolo:
Mass spectrometic detection for capillary isoelectric focusing separationsof complex protein mixtures
Autore:
Jensen, PK; Pasa-Tolic, L; Peden, KK; Martinovic, S; Lipton, MS; Anderson, GA; Tolic, N; Wong, KK; Smith, RD;
Indirizzi:
Pacific NW Labs, Environm Mol Sci Lab, Richland, WA 99352 USA Pacific NW Labs Richland WA USA 99352 Mol Sci Lab, Richland, WA 99352 USA
Titolo Testata:
ELECTROPHORESIS
fascicolo: 7, volume: 21, anno: 2000,
pagine: 1372 - 1380
SICI:
0173-0835(200004)21:7<1372:MSDFCI>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI K-12; 2-DIMENSIONAL ELECTROPHORESIS; IDENTIFICATION; PROTEOMES; MS; QUANTITATION; MOBILIZATION; TRANSFERRIN; GENOME;
Keywords:
capillary isoelectric focusing Fourier transform ion cyclotron resonance mass spectrometry; proteome; complex biological mixture separation; Deinococcus radiodurans; Escherichia coli;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Smith, RD Pacific NW Labs, Environm Mol Sci Lab, POB 999,Mail Stop K8-98, Richland, WA 99352 USA Pacific NW Labs POB 999,Mail Stop K8-98 Richland WA USA 99352 SA
Citazione:
P.K. Jensen et al., "Mass spectrometic detection for capillary isoelectric focusing separationsof complex protein mixtures", ELECTROPHOR, 21(7), 2000, pp. 1372-1380

Abstract

Capillary isoelectric focusing (CIEF) can provide high-resolution separations of complex protein mixtures, but until recently it has primarily been used with conventional UV detection. This technique would be greatly enhanced by much more information-rich detection methods that can aid in protein characterization. We describe progress in the development of the combinationof CIEF with Fourier transform ion cyclotron resonance (FTICR) mass spectrometry and its application to proteome characterization. Studies have revealed 400-1000 putative proteins in the mass range of 2-100 kDa from total injections of similar to 300 ng protein in single CIEF-FTICR analyses of celllysates for both Escherichia coli (E. coli) and Deinococcus radiodurans (D. radiodurans). We also demonstrate the use of isotope labeling of the cellgrowth media to improve mass measurement accuracy and provide a means for quantitative proteome-wide measurements of protein expression. The ability to make such comprehensive and precise measurements of differences in protein expression in response to cellular perturbations should provide new insights into complex cellular processes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 23:24:01