期刊
JOURNAL OF PROTEOME RESEARCH
卷 8, 期 5, 页码 2201-2210出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr800654s
关键词
mass spectrometry; post-translational modification; full-length protein standard; stable isotope
资金
- NIH/NIGMS Cell Cycle Regulation [2 R01 GM039023]
- Helen Hay Whitney Foundation
- International Rett Syndrome Foundation
Measurements of protein abundance and quantitative assessment of multiple post-translational modifications (PTMs) within a single protein are increasingly used to understand the control of protein activity, particularly in metazoan cells. General methods of wide applicability and precision/accuracy for quantitative estimation of protein post-translational regulation are lacking. Protein mass spectrometry has evolved from a high-throughput qualitative technique to a potentially general quantitative tool, but there are still serious limitations in dynamic range and coverage. To address some of these limitations, we introduce a novel MS-based quantitative strategy, FLEXIQuant, (Full-Length Expressed Stable Isotope-labeled Proteins for Quantification), which can track changes in relative peptide abundances as a function of PTM, and determine absolute quantity of a protein from its lysate. We examined two subunits of the anaphase-promoting complex, CDC27 and APC5, as a test of our ability to monitor quantitatively, the PTM status of several peptides over time. We find evidence of differential regulation at different sites, a phenomenon we believe will be very widespread. FLEXIQuant proved itself to be capable of serving as a general quantitative tool.
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