Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Rapid quantitative measurements of proteomes by Fourier transform ion cyclotron resonance mass spectrometry
Autore:
Smith, RD; Pasa-Tolic, L; Lipton, MS; Jensen, PK; Anderson, GA; Shen, YF; Conrads, TP; Udseth, HR; Harkewicz, R; Belov, ME; Masselon, C; Veenstra, TD;
Indirizzi:
Pacific NW Natl Lab, Environm Mol Sci Lab, Richland, WA 99352 USA Pacific NW Natl Lab Richland WA USA 99352 Sci Lab, Richland, WA 99352 USA
Titolo Testata:
ELECTROPHORESIS
fascicolo: 9, volume: 22, anno: 2001,
pagine: 1652 - 1668
SICI:
0173-0835(200105)22:9<1652:RQMOPB>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTROSPRAY-IONIZATION; 2-DIMENSIONAL ELECTROPHORESIS; PROTEIN IDENTIFICATION; SEQUENCE DATABASES; INFORMATION; EXPRESSION; MIXTURES; UTILITY; GELS;
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:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Smith, RD Pacific NW Natl Lab, Environm Mol Sci Lab, POB 999,Mail Stop K8-98, Richland, WA 99352 USA Pacific NW Natl Lab POB 999,Mail Stop K8-98 Richland WA USA 99352
Citazione:
R.D. Smith et al., "Rapid quantitative measurements of proteomes by Fourier transform ion cyclotron resonance mass spectrometry", ELECTROPHOR, 22(9), 2001, pp. 1652-1668

Abstract

The patterns of gene expression, post-translational modifications, protein/biomolecular interactions, and how these may be affected by changes in theenvironment, cannot be accurately predicted from DNA sequences. Approachesfor proteome characterization are generally based upon mass spectrometric analysis of in-gel digested two dimensional polyacrylamide gel electrophoresis (2-D PAGE) separated proteins, allowing relatively rapid protein identification compared to conventional approaches. This technique, however, is constrained by the speed of the 2-D PAGE separations, the sensitivity limitsintrinsic to staining necessary for protein visualization, the speed and sensitivity of subsequent mass spectrometric analyses for identification, and the limited ability for accurate quantitative measurements based on differences in spot intensity. We are presently developing alternative approaches for proteomics based upon the combination of fast capillary electrophoresis, or other suitable chromatographic separations, and the high mass accuracy and sensitivity obtainable with unique Fourier transform ion cyclotron resonance (FTICR) mass spectrometers available at our laboratory. Several approaches are presently being pursued; one based upon the analysis of intactproteins and the second upon approaches for global protein digestion and accurate peptide mass analysis. Quantitation of protein/peptide levels are based on using two or more stable-isotope labeled versions of proteomes which are combined to obtain precise quantitation of relative protein abundances. We describe the status of our efforts towards the development of a high-throughput proteomics capability and present initial results for application to several microorganisms and discuss our efforts for extending the developed capability to mammalian proteomes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 15:22:52