Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-05

AUTHORS

Huilin Zhou, Jeffrey A. Ranish, Julian D. Watts, Ruedi Aebersold

ABSTRACT

The adaptation of sequences of chemical reactions to a solid-phase format has been essential to the automation, reproducibility, and efficiency of a number of biotechnological processes including peptide and oligonucleotide synthesis and sequencing1,2,3,4. Here we describe a method for the site-specific, stable isotopic labeling of cysteinyl peptides in complex peptide mixtures through a solid-phase capture and release process, and the concomitant isolation of the labeled peptides. The recovered peptides were analyzed by microcapillary liquid chromatography and tandem mass spectrometry (μLC-MS/MS) to determine their sequences and relative quantities. The method was used to detect galactose-induced changes in protein abundance in the yeast Saccharomyces cerevisiae. A side-by-side comparison with the isotope-coded affinity tag (ICAT) method5 demonstrated that the solid-phase method for stable isotope tagging of peptides is comparatively simpler, more efficient, and more sensitive. More... »

PAGES

512-515

Journal

TITLE

Nature Biotechnology

ISSUE

5

VOLUME

20

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt0502-512

    DOI

    http://dx.doi.org/10.1038/nbt0502-512

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1023426571

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11981568


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