期刊
JOURNAL OF MASS SPECTROMETRY
卷 43, 期 4, 页码 518-527出版社
WILEY
DOI: 10.1002/jms.1342
关键词
MALDI-TOF; phosphopeptides; quantification; calibration; ionization
资金
- NCI NIH HHS [F32 CA117672, F32 CA117672-02, F32 CA117672A] Funding Source: Medline
- NHGRI NIH HHS [R01 HG003864] Funding Source: Medline
Despite advances in methods and instrumentation for analysis of phosphopeptides using mass spectrometry, it is still difficult to quantify the extent of phosphorylation of a substrate because of physiochemical differences between unphosphorylated and phosphorylated peptides. Here we report experiments to investigate those differences using MALDI-TOF mass spectrometry for a set of synthetic peptides by creating calibration curves of known input ratios of peptides/phosphopeptides and analyzing their resulting signal intensity ratios. These calibration curves reveal subtleties in sequence-dependent differences for relative desorption/ionization efficiencies that cannot be seen from single-point calibrations. We found that the behaviors were reproducible with a variability of 5-10% for observed phosphopeptide signal. Although these data allow us to begin addressing the issues related to modeling these properties and predicting relative signal strengths for other peptide sequences, it is clear that this behavior is highly complex and needs to be further explored. Copyright (C) 2007 John Wiley & Sons, Ltd.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据