Sub parts-per-million mass measurement accuracy of intact proteins and product ions achieved using a dual electrospray ionization quadrupole fourier transform ion cyclotron resonance mass spectrometer.
Sub parts-per-million mass measurement accuracy of intact proteins and product ions achieved using a dual electrospray ionization quadrupole fourier transform ion cyclotron resonance mass spectrometer.
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使用双电喷雾电离四极傅里叶变换离子回旋共振质谱仪实现完整蛋白质和产物离子的百万分之一质量测量精度。
DOI：
10.1016/j.jasms.2006.08.014
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发表时间：
2007
影响因子：
3.2
通讯作者：
Muddiman,DavidC
中科院分区：
文献类型：
--
作者：
WilliamsJr,DKeith;Hawkridge,AdamM;Muddiman,DavidC
高质量测量精度（MMA）证明了完整的蛋白质和随后的碰撞诱导解离产物离子使用内部校准。采用双电喷雾电离源和混合四极傅里叶变换离子回旋共振质谱仪（Q-FT-ICR）进行内标。最初，经由第一电喷雾（ESI）发射器产生的分析物离子在外部四极中被隔离和解离。该事件之后是同时切换到校准离子ESI发射器和禁用外部四极杆的隔离和激活，使得在将分析物/校准离子混合物注入ICR池之前累积宽范围的校准离子。在这些研究中使用了两种不同的内部校准溶液，以评估蜂毒肽和泛素的自上而下表征方法。虽然蛋白质片段的外部校准导致绝对MMA大于16 ppm，但内部标准化显着改善了完整蛋白质及其产物离子的MMA，其范围为−2.0 ppm至1.1 ppm，平均值为−0.9 ppm。该方法需要对ESI-FT-ICR质谱仪进行有限的修改，并且适用于正离子化和负离子化模式。
High mass measurement accuracy (MMA) is demonstrated for intact proteins and subsequent collision-induced dissociation product ions using internal calibration. Internal calibration was accomplished using a dual electrospray ionization source coupled with a hybrid quadrupole Fourier transform ion cyclotron resonance (Q-FT-ICR) mass spectrometer. Initially, analyte ions generated via the first electrospray (ESI) emitter are isolated and dissociated in the external quadrupole. This event is followed by a simultaneous switch to the calibrant ion ESI emitter and a disablement of the isolation and activation of the external quadrupole such that a broadm/zrange of calibrant ions are accumulated before injecting the analyte/calibrant ion mixture into the ICR cell. Two different internal calibrant solutions were utilized in these studies to evaluate this approach for the top-down characterization of melittin and ubiquitin. While external calibration of protein fragments resulted in absolute MMA greater than 16 ppm, internal standardization significantly improved upon the MMA of both the intact proteins and their products ions which ranged from −2.0 ppm to 1.1 ppm, with an average of −0.9 ppm. This method requires limited modification to ESI-FT-ICR mass spectrometers and is applicable for both positive and negative ionization modes.