Selective isolation of multiply charged peptides: a confident strategy for protein identification using a linear trap quadrupole mass spectrometer.
Eur J Mass Spectrom (Chichester)
; 18(6): 505-8, 2012.
Article
em En
| MEDLINE
| ID: mdl-23654195
In this work, a method devised for the selective isolation of multiply-charged peptide applied to a complex protein mixture was evaluated for the first time using a mass spectrometer with low resolution (LTQ). In this procedure, all primary amino groups of tryptic peptides derived from human Liver tissue interstitial fluid (TIF) are blocked, restricting their positive charge, at acidic pH, to the presence of histidine and arginine residues. After strong cation exchange chromatography, multiply-charged peptides (#R+#H > 1) are retained in the column and separated with high selectivity from singly (#R+#H = 1) and neutral peptides (#R +#H = 0) which are collected together in the flow-through. Using Liquid chromatography electrospray ionization tandem mass spectrometry analysis the retained fraction displayed a 95% enrichment of multiply charged peptides while in the flow-through; only 4% of multiply-charged peptides were identified.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Proteoma
/
Espectrometria de Massas por Ionização por Electrospray
/
Líquido Extracelular
/
Fígado
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Revista:
Eur J Mass Spectrom (Chichester)
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Cuba
País de publicação:
Reino Unido