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Titolo:
Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fourier transform ion cyclotron resonance mass spectrometry
Autore:
Martin, SE; Shabanowitz, J; Hunt, DF; Marto, JA;
Indirizzi:
Univ Virginia, Dept Chem, Charlottesville, VA 22904 USA Univ Virginia Charlottesville VA USA 22904 Charlottesville, VA 22904 USA
Titolo Testata:
ANALYTICAL CHEMISTRY
fascicolo: 18, volume: 72, anno: 2000,
pagine: 4266 - 4274
SICI:
0003-2700(20000915)72:18<4266:SMAMPS>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-CAPTURE DISSOCIATION; PROTEIN IDENTIFICATION; CAPILLARY-ELECTROPHORESIS; MICROFABRICATED DEVICE; DELAYED EXTRACTION; COMPLEX PEPTIDE; INNER DIAMETERS; IONIZATION; CHROMATOGRAPHY; SENSITIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
79
Recensione:
Indirizzi per estratti:
Indirizzo: Hunt, DF Univ Virginia, Dept Chem, Mccormick Rd, Charlottesville, VA 22904USA Univ Virginia Mccormick Rd Charlottesville VA USA 22904 22904 USA
Citazione:
S.E. Martin et al., "Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fourier transform ion cyclotron resonance mass spectrometry", ANALYT CHEM, 72(18), 2000, pp. 4266-4274

Abstract

Subfemtomole peptide sequence analysis has been achieved using microcapillary HPLC columns, with integrated nanoelectrospray emitters, coupled directly to a Fourier transform ion cyclotron resonance mass spectrometer. Accurate mass (+/-0.010 Da) peptide maps are generated from a standard six-protein digest mixture, whose principle components span a concentration dynamic range of 1000:1. Iterative searches against similar to 189 000 entries in the OWL database readily identify each protein, with high sequence coverage (20-60%), from as little as 10 amol loaded on-column. In addition, a simple variable-flow HPLC apparatus provides for on-line tandem mass spectrometricanalysis of tryptic peptides at the 400-amol level. MS/MS data are searched against similar to 280 000 entries in a nonredundant protein database using SEQUEST. Accurate precursor and product ion mass information readily identifiers primary amino acid sequences differing by:asparagine vs aspartic acid (Delta m = 0.98 Da) and glutamine vs lysine (Delta m = 0.036 Da).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 21:41:37