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Titolo:
Simplification of complex peptide mixtures for proteomic analysis: Reversible biotinylation of cysteinyl peptides
Autore:
Spahr, CS; Susin, SA; Bures, EJ; Robinson, JH; Davis, MT; McGinley, MD; Kroemer, G; Patterson, SD;
Indirizzi:
Amgen Inc, Thousand Oaks, CA 91320 USA Amgen Inc Thousand Oaks CA USA 91320 gen Inc, Thousand Oaks, CA 91320 USA CNRS, Villejuif, France CNRS Villejuif FranceCNRS, Villejuif, France
Titolo Testata:
ELECTROPHORESIS
fascicolo: 9, volume: 21, anno: 2000,
pagine: 1635 - 1650
SICI:
0173-0835(200005)21:9<1635:SOCPMF>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANDEM MASS-SPECTROMETRY; AMINO-ACID-SEQUENCES; PROTEIN DATABASE; IDENTIFICATION; APOPTOSIS; LEVEL; GEL;
Keywords:
affinity chromatography; cysteine biotinylation; mass spectrometer; mitochondria; apoptosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Patterson, SD Amgen Inc, 1 Amgen Ctr Dr,MS 14-2-E, Thousand Oaks, CA 91320USA Amgen Inc 1 Amgen Ctr Dr,MS 14-2-E Thousand Oaks CA USA 91320
Citazione:
C.S. Spahr et al., "Simplification of complex peptide mixtures for proteomic analysis: Reversible biotinylation of cysteinyl peptides", ELECTROPHOR, 21(9), 2000, pp. 1635-1650

Abstract

A rapid means of identifying many components in an enriched mixture of proteins is enzymatic digestion of the entire protein fraction. This complex peptide mixture is then subjected to reversed-phase high performance liquid chromatography (HPLC) coupled on-line with a mass spectrometer capable of data-dependent ion selection for fragmentation (LC-tandem mass spectrometry;MS/MS). Thus, as many peptides as possible in the sample are fragmented toproduce MS/MS spectra, which can then be searched against sequence databases. Ideally, one peptide from each protein in the mixture would be fragmented and identified. To this end, we employed an affinity selection method tocapture cysteinyl peptides and thereby simplify the mixture. Both the captured cysteinyl and the noncysteinyl peptides are analyzed by LC-MS/MS, to increase the numer of proteins identified. The method was tested on a limited set of standard proteins and applied to the analysis of a protein fraction obtained from isolated mitochondria treated with atractyloside. To further increase the number of different precursor ions selected for fragmentation, dynamic exclusion and ion selection from multiple narrow mass ranges of consecutive runs were employed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 04:03:01