Journal
ANALYTICAL CHEMISTRY
Volume 78, Issue 13, Pages 4271-4280Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac0600050
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- NIGMS NIH HHS [5T32 GM 08276] Funding Source: Medline
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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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