scholarly journals Design considerations for high speed quantitative mass spectrometry with MALDI ionization

2006 ◽  
Vol 17 (8) ◽  
pp. 1129-1141 ◽  
Author(s):  
Jay J. Corr ◽  
Peter Kovarik ◽  
Bradley B. Schneider ◽  
Jan Hendrikse ◽  
Alexander Loboda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Speed ◽  
Quantitative Mass Spectrometry ◽  
Design Considerations ◽  
Maldi Ionization

Rapid Online Buffer Exchange: A Method for Screening of Proteins, Protein Complexes, and Cell Lysates by Native Mass Spectrometry

2019 ◽  
Author(s):  
Zachary VanAernum ◽  
Florian Busch ◽  
Benjamin J. Jones ◽  
Mengxuan Jia ◽  
Zibo Chen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Speed ◽  
Structural Information ◽  
Protein Complexes ◽  
High Sensitivity ◽  
Native Mass Spectrometry ◽  
Structural Features ◽  
Consumer Products ◽  
Cell Lysates ◽  
Protein Expression And Purification

It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer products, chemical processes, and therapeutics. Native mass spectrometry (nMS) has become an important tool in protein analysis due to its ability to retain non-covalent interactions during measurements, making it possible to obtain protein structural information with high sensitivity and at high speed. Interferences from the presence of non-volatiles are typically alleviated by offline buffer exchange, which is timeconsuming and difficult to automate. We provide a protocol for rapid online buffer exchange (OBE) nMS to directly screen structural features of pre-purified proteins, protein complexes, or clarified cell lysates. Information obtained by OBE nMS can be used for fast (<5 min) quality control and can further guide protein expression and purification optimization.

P3-182: Identification of target engagement biomarkers for MARK inhibitor discovery using quantitative mass spectrometry

2010 ◽  
Vol 6 ◽  
pp. S504-S504
Author(s):  
Mansuo Hayashi ◽  
Cloud Paweletz ◽  
Shang-Shuan Yu ◽  
Hugh Nuthall ◽  
Alan Northrup ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Target Engagement ◽  
Quantitative Mass Spectrometry ◽  
Inhibitor Discovery

Time-Resolved Micro Liquid Desorption Mass Spectrometry: Mechanism, Features, and Kinetic Applications

2006 ◽  
Vol 59 (2) ◽  
pp. 81 ◽  
Author(s):  
Ales Charvat ◽  
Andreas Bógehold ◽  
Bernd Abel
Keyword(s):  
Mass Spectrometry ◽  
Liquid Phase ◽  
High Speed ◽  
High Performance ◽  
Kinetic Studies ◽  
Solution Concentration ◽  
Bulk Water ◽  
Laser Wavelength ◽  
Time Resolved ◽  
Desorption Mass Spectrometry

Liquid water beam desorption mass spectrometry is an intriguing technique to isolate charged molecular aggregates directly from the liquid phase and to analyze them employing sensitive mass spectrometry. The liquid phase in this approach consists of a 10 µm diameter free liquid filament in vacuum which is irradiated by a focussed infrared laser pulse resonant with the OH-stretch vibration of bulk water. Depending upon the laser wavelength, charged (e.g. protonated) macromolecules are isolated from solution through a still poorly characterized mechanism. After the gentle liquid-to-vacuum transfer the low-charge-state aggregates are analyzed using time-of-flight mass spectrometry. A recent variant of the technique uses high performance liquid chromatography valves for local liquid injections of samples in the liquid carrier beam, which enables very low sample consumption and high speed sample analysis. In this review we summarize recent work to characterize the ‘desorption’ or ion isolation mechanism in this type of experiment. A decisive and interesting feature of micro liquid beam desorption mass spectrometry is that — under certain conditions — the gas-phase mass signal for a large number of small as well as supramolecular systems displays a surprisingly linear response on the solution concentration over many orders of magnitude, even for mixtures and complex body fluids. This feature and the all-liquid state nature of the technique makes this technique a solution-type spectroscopy that enables real kinetic studies involving (bio)polymers in solution without the need for internal standards. Two applications of the technique monitoring enzyme digestion of proteins and protein aggregation of an amyloid model system are highlighted, both displaying its potential for monitoring biokinetics in solution.

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