scholarly journals Experimental Strategies for Avoiding Saturation Effects in ESI-MS

2019 ◽  
Author(s):  
Alan Wei ◽  
Anuj Joshi ◽  
Yuxuan Chen ◽  
J Scott McIndoe

<p>All instruments with detectors are prone to saturation effects at high concentration, and mass spectrometers are no exception. The very high sensitivity of mass spectrometry makes the onset of saturation occur at lower concentrations than other methods, and in cases where the analyte of interest is very reactive, concentrations at which saturation can be problematic may be necessary in order to ensure decomposition is mitigated. Indications that saturation is occurring are provided, and some data processing strategies are outlined, followed by a range of detuning strategies that may be employed to reduce saturation effects in the context of electrospray ionization mass spectrometry (ESI-MS), including lowering voltages on detector or capillary, increasing cone gas flow rates, or adjusting the probe position. A combination of strategies generally allows researchers to make the best possible compromises when studying compounds at relatively high concentration.</p>

2019 ◽  
Author(s):  
Alan Wei ◽  
Anuj Joshi ◽  
Yuxuan Chen ◽  
J Scott McIndoe

<p>All instruments with detectors are prone to saturation effects at high concentration, and mass spectrometers are no exception. The very high sensitivity of mass spectrometry makes the onset of saturation occur at lower concentrations than other methods, and in cases where the analyte of interest is very reactive, concentrations at which saturation can be problematic may be necessary in order to ensure decomposition is mitigated. Indications that saturation is occurring are provided, and some data processing strategies are outlined, followed by a range of detuning strategies that may be employed to reduce saturation effects in the context of electrospray ionization mass spectrometry (ESI-MS), including lowering voltages on detector or capillary, increasing cone gas flow rates, or adjusting the probe position. A combination of strategies generally allows researchers to make the best possible compromises when studying compounds at relatively high concentration.</p>


2009 ◽  
Vol 31 (5) ◽  
pp. 30-33
Author(s):  
Tony Postle

Advances in the design of electrospray ionization–mass spectrometry (ESI-MS) over recent years have revolutionized approaches to the study of lipids and lipid metabolism. In additional to providing compositional information in great detail and at high sensitivity, with minimal sample preparation, ESI-MS coupled with the incorporation of substrates labelled with stable isotopes permits the analysis of rates of synthesis and turnover of individual lipid molecular species. Also, being non-radioactive, this technology is readily used in clinical studies to probe disease mechanisms directly.


2020 ◽  
Author(s):  
Danye Qiu ◽  
Miranda S. Wilson ◽  
Verena B. Eisenbeis ◽  
Robert K. Harmel ◽  
Esther Riemer ◽  
...  

AbstractThe analysis of myo-inositol phosphates (InsPs) and myo-inositol pyrophosphates (PP-InsPs) is a daunting challenge due to the large number of possible isomers, the absence of a chromophore, the high charge density, the low abundance, and the instability of the esters and anhydrides. Given their importance in biology, an analytical approach to follow and understand this complex signaling hub is highly desirable. Here, capillary electrophoresis (CE) coupled to electrospray ionization mass spectrometry (ESI-MS) is implemented to analyze complex mixtures of InsPs and PP-InsPs with high sensitivity. Stable isotope labeled (SIL) internal standards allow for matrix-independent quantitative assignment. The method is validated in wild-type and knockout mammalian cell lines and in model organisms. SIL-CE-ESI-MS enables for the first time the accurate monitoring of InsPs and PP-InsPs arising from compartmentalized cellular synthesis pathways, by feeding cells with either [13C6]-myo-inositol or [13C6]-D-glucose. In doing so, we uncover that there must be unknown inositol synthesis pathways in mammals, highlighting the unique potential of this method to dissect inositol phosphate metabolism and signalling.


RSC Advances ◽  
2018 ◽  
Vol 8 (31) ◽  
pp. 17293-17299 ◽  
Author(s):  
Wei Kou ◽  
Hua Zhang ◽  
Aisha Bibi ◽  
Mufang Ke ◽  
Jing Han ◽  
...  

A simple, fast and high-sensitivity method for quantification of fluoroquinolones in environmental water samples using MIPs-iEESI-MS.


Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 4979
Author(s):  
Marco Giampà ◽  
Elvira Sgobba

Noncovalent interactions are the keys to the structural organization of biomolecule e.g., proteins, glycans, lipids in the process of molecular recognition processes e.g., enzyme-substrate, antigen-antibody. Protein interactions lead to conformational changes, which dictate the functionality of that protein-protein complex. Besides biophysics techniques, noncovalent interaction and conformational dynamics, can be studied via mass spectrometry (MS), which represents a powerful tool, due to its low sample consumption, high sensitivity, and label-free sample. In this review, the focus will be placed on Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS) and its role in the analysis of protein-protein noncovalent assemblies exploring the relationship within noncovalent interaction, conformation, and biological function.


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