Liquid phase interfacing and miniaturization in matrix-assisted laser desorption/ionization mass spectrometry

Foret, František; Preisler, Jan

doi:10.1002/1615-9861(200204)2:4<360::aid-prot360>3.0.co;2-y

Cited by 57 publications

(37 citation statements)

References 123 publications

(142 reference statements)

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“…A high number of references showed the off-line use of CE-techniques with matrix-assisted laser desorption/ionization (MALDI) after deposition of the eluting sample on a matrix. For further details on this specific hyphenation type the readers are referred to specific articles and reviews [23][24][25]. ESI is found in all of the applications listed in Table 4 and this ionization type is now described more in detail.…”

Section: Interfacing Ce To Msmentioning

confidence: 99%

Capillary electrophoresis – mass spectrometry: 15 years of developments and applications

Schmitt‐Kopplin¹,

Frommberger²

2003

Electrophoresis

282

232

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Capillary electrophoresis -mass spectrometry: 15 years of developments and applicationsSince its introduction in 1987, capillary electrophoresis-mass spectrometry (CE-MS) has developed to a well accepted multidimensional analytical approach complementary and/or competitive to classical MS-hyphenated separation techniques. The threefold combination of rapid developments of an exceptional separation technique, of selective mass detection possibilities, and of very mild ionization modes first allowed these progresses. This article shows the CE specificities that need to be well controlled/known, compared to classical and more routinely used liquid chromatography in the light of its coupling to MS. The major trends and developments over the last 15 years and most of the reviews and applications found in ISI Web of science and publisher databases are presented in a tabulated way. The reader can thus rapidly find existing CE-MS analysis techniques in his field of research and application (forensics, environment, bioanalytics, pharmaceutics, and metabolites).

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Section: Interfacing Ce To Msmentioning

confidence: 99%

Capillary electrophoresis – mass spectrometry: 15 years of developments and applications

Schmitt‐Kopplin¹,

Frommberger²

2003

Electrophoresis

282

232

View full text Add to dashboard Cite

show abstract

“…This paragraph will not deal with this emerging technology any further since quantitative measurements are difficult to perform with MALDI-MS, especially when coupled to separation techniques (i.e., spreading out the analyte over several spots). A detailed review about MALDI interfaces was published in [38].…”

Section: Other Interfacesmentioning

confidence: 99%

Quantitation in capillary electrophoresis-mass spectrometry

2005

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Quantitation in capillary electrophoresis-mass spectrometryCE-MS has evolved into a strong alternative to LC-MS. Most of CE-MS applications deal with characterization and identification. However, quantitative aspects have gained importance in, e.g., pharmaceutical and biotechnological applications. Here we summarize and evaluate various methodological aspects in order to achieve sensitive and reproducible results. Similar to LC-MS, aspects of matrix influence on the electrospray process need to be carefully addressed when quantitative results are intended by CE-MS. Due to a more complicated coupling special emphasis needs to be put on the CE-MS interface. Generally linearity over more than three orders of magnitude can be achieved by CE-ESI-MS. Furthermore, a literature survey has been performed in order to give an overview over quantitative measurements performed by CE-MS. The precision can be doubled when changing from a structural related to an isotopically labeled internal standard. Thus a level of precision better than 5% RSD can be achieved.

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“…However, with the introduction of seamless integration of LC and matrix spotting systems, it is now also possible to combine peptide separation by LC with MALDI. 12 Step three, mass analysis, can be achieved in time with ion trap mass spectrometers that are commonly coupled to LC-ESI systems, or in space with time-of-flight (TOF) mass spectrometers that are commonly coupled to MALDI systems. Thus it is now possible to combine the power of peptide separation by LC with the high resolution of MALDI-TOF-TOF instruments.…”

Section: A Quantitative Proteomic Methods Using Liquid Chromatography-mentioning

confidence: 99%

Liquid chromatography with tandem mass spectrometry-based proteomic discovery in aging and Alzheimer’s disease

Montine

Woltjer

Pan

et al. 2006

NeuroRX

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Summary: Systems biology offers enormous potential to understand the complexity of human brain aging and neurodegenerative diseases. Proteomics has an important role in these investigations because of its unique strengths and because of the potential central pathogenic contribution of pathological protein to several of these diseases. Here we have reviewed the methods and presented some examples of liquid chromatography-electrospray ionization-tandem mass spectrometrybased proteomics, with and without quantification using isotope-coded affinity tags, in the investigation of aging and Alzheimer's disease. As protocols and methods for improved quantitative high-throughput proteomics constantly improve, this approach will likely continue to provide deeper insight into human brain aging and neurodegenerative diseases.

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Liquid phase interfacing and miniaturization in matrix-assisted laser desorption/ionization mass spectrometry

Abstract: Mass spectrometry is becoming the major analytical tool in biology research. This short review summarizes the state-of-the-art in the interface miniaturization and strategies for analysis of limited sample amounts by matrix assisted laser desorption/ionization mass spectrometry.

Cited by 57 publications

References 123 publications

Capillary electrophoresis – mass spectrometry: 15 years of developments and applications

Capillary electrophoresis – mass spectrometry: 15 years of developments and applications

Quantitation in capillary electrophoresis-mass spectrometry

Liquid chromatography with tandem mass spectrometry-based proteomic discovery in aging and Alzheimer’s disease

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