离子淌度-飞行时间质谱测量中低于飞摩尔级别的肽段检测
Sub-femtomole peptide detection in ion mobility-time-of-flight mass spectrometry measurements.
作者信息
McLean John A, Russell David H
机构信息
Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.
出版信息
J Proteome Res. 2003 Jul-Aug;2(4):427-30. doi: 10.1021/pr034004p.
Sensitivity and detection limit enhancements are obtained for peptides by performing high repetition rate (150 Hz) matrix-assisted laser desorption/ionization (MALDI) coupled with ion mobility-time-of-flight mass spectrometry. Absolute limits of detection (3sigma) for model peptides are on the order of 0.1 fmol of peptide deposited and represent a factor of 40-60 improvement over data obtained using typical low repetition (20 Hz) MALDI. This increase in sensitivity is demonstrated for two-dimensional MALDI-IM-TOFMS peptide mass mapping of bovine hemoglobin.
通过执行高重复率（150赫兹）的基质辅助激光解吸/电离（MALDI）并结合离子淌度-飞行时间质谱，可提高肽段的灵敏度和检测限。模型肽段的绝对检测限（3σ）约为沉积肽段的0.1飞摩尔，相较于使用典型低重复率（20赫兹）MALDI获得的数据，有40至60倍的提升。牛血红蛋白的二维MALDI-IM-TOFMS肽质量图谱证明了这种灵敏度的提高。
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