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Titolo:
Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry
Autore:
Shi, SDH; Hemling, ME; Carr, SA; Horn, DM; Lindh, I; McLafferty, FW;
Indirizzi:
SmithKline Beecham Pharmaceut PLC, Dept Phys & Struct Chem, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut PLC King Of Prussia PA USA 19406 19406 USA Cornell Univ, Baker Lab Chem, Ithaca, NY 14853 USA Cornell Univ Ithaca NYUSA 14853 iv, Baker Lab Chem, Ithaca, NY 14853 USA
Titolo Testata:
ANALYTICAL CHEMISTRY
fascicolo: 1, volume: 73, anno: 2001,
pagine: 19 - 22
SICI:
0003-2700(20010101)73:1<19:PMBECD>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
INFRARED MULTIPHOTON DISSOCIATION; MULTIPLY-CHARGED IONS; PROTEIN-PHOSPHORYLATION; SELECTIVE DETECTION; PHOSPHOPEPTIDES; IDENTIFICATION; PEPTIDES; SITES; CHROMATOGRAPHY; LOCALIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Hemling, ME SmithKline Beecham Pharmaceut PLC, Dept Phys & Struct Chem, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut PLC King Of Prussia PA USA 19406
Citazione:
S.D.H. Shi et al., "Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry", ANALYT CHEM, 73(1), 2001, pp. 19-22

Abstract

Of methods for dissociation of multiply charged peptide and protein ions, electron capture dissociation (ECD) has the advantages of cleaving between a high proportion of amino acids, without loss of such posttranslational modifications as glycosylation and carboxylation, Here this capability is successfully extended to phosphorylation, for which collisionally activated dissociation (CAD) can cause extensive loss of H3PO4 and HPO3, As shown here,these losses are minimal in ECD spectra, an advantage for measuring the degree of phosphorylation. For phosphorylated peptides, ECD and CAD spectra give complementary backbone cleavages for identifying modification sites. For a 24-kDa heterogeneous phosphoprotein, bovine beta -casein, activated ionECD cleaved 87 of 208 backbone bonds that identified a phosphorylation site at Ser-15, and localized three more among Ser-17,-18, -19, and -22 and Thr-24, and the last among four other sites: This is the first direct site-specific characterization of this key post-translational modification on a protein without its prior degradation, such as proteolysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 14:21:40