Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: human histone H4.
Anal Chem
; 78(13): 4271-80, 2006 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-16808433
ABSTRACT
Here we show that fragment ion abundances from dissociation of ions created from mixtures of multiply modified histone H4 (11 kDa) or of N-terminal synthetic peptides (2 kDa) correspond to their respective intact ion abundances measured by Fourier transform mass spectrometry. Isomeric mixtures of modified forms of the same protein are resolved and quantitated with a precision of =5% using the relative ratios of their fragment ions, with intact protein ions created by electrospray greatly easing many of the systematic biases that more strongly affect small peptides (e.g., differences in ionization efficiency and ion m/z values). The ion fragmentation methods validated here are directly extensible to intact human proteins to derive quantitative information on the highly related and often isomeric protein forms created by combinatorial arrays of posttranslational modifications.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Histonas
/
Isoformas de Proteínas
/
Espectrometria de Massas em Tandem
Limite:
Humans
Idioma:
En
Revista:
Anal Chem
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Estados Unidos