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Measurement of the isotope enrichment of stable isotope-labeled proteins using high-resolution mass spectra of peptides

Academic Article
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Overview

authors

  • MacCoss, M. J.
  • Wu, Chunlei
  • Matthews, D. E.
  • Yates III, John

publication date

  • December 2005

journal

  • Analytical Chemistry  Journal

abstract

  • Stable isotope-enriched molecules are used as internal standards and as tracers of in vivo substrate metabolism. The accurate conversion of measured ratios in the mass spectrometer to mole ratios is complicated because a polyatomic molecule containing enriched atoms will result in a combinatorial distribution of isotopomers depending on the enrichment and number of "labeled" atoms. This effect could potentially cause a large error in the mole ratio measurement depending on which isotope peak or peaks were used to determine the ratio. We report a computational method that predicts isotope distributions over a range of enrichments and compares the predicted distributions to experimental peptide isotope distributions obtained by Fourier transform ion cyclotron resonance mass spectrometry. Our approach is accurate with measured enrichments within 1.5% of expected isotope distributions. The method is also precise with 4.9, 2.0, and 0.8% relative standard deviations for peptides containing 59, 79, and 99 atom % excess (15)N, respectively. The approach is automated making isotope enrichment calculations possible for thousands of peptides in a single muLC-FTICR-MS experiment.

subject areas

  • Animals
  • Gas Chromatography-Mass Spectrometry
  • Isotopes
  • Liver
  • Male
  • Peptides
  • Proteins
  • Rats
  • Rats, Sprague-Dawley
  • Saccharomyces cerevisiae
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Identity

International Standard Serial Number (ISSN)

  • 0003-2700

Digital Object Identifier (DOI)

  • 10.1021/ac0508393

PubMed ID

  • 16316172
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Additional Document Info

start page

  • 7646

end page

  • 7653

volume

  • 77

issue

  • 23

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