Trends in CE‐MS 2005–2006

Gaspar, Andras; Englmann, Matthias; Fekete, Ágnes; Harir, Mourad; Schmitt‐Kopplin, Philippe

doi:10.1002/elps.200700721

Cited by 73 publications

(57 citation statements)

References 187 publications

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“…The method of choice for coupling CE to ESI/MS is the coaxial sheath-flow interfacing, which is stable, and provides the best sensitivity (in the amol range). Stability and sensitivity of this interfacing has been confirmed by a number of studies (Gaspar, et al, 2008;Haselberg, et al, 2007;HernandezBorges, et al, 2007;Tempels, et al, 2007). We have shown that under certain conditions , KSPs will move faster in CE than non-KSPs.…”

Section: Using Capillary Electrophoresis To Identify the Proteome Of supporting

confidence: 73%

“…However, this disadvantage can be overcome by using other detectors. The sensitivity of LIF is subnanomolar (Gutman & Kessler, 2006) and a MS detector could provide amol-range sensitivity (Gaspar, Englmann, Fekete, Harir, & Schmitt-Kopplin, 2008;Haselberg, de Jong, & Somsen, 2007;Hernandez-Borges, Borges-Miquel, RodriguezDelgado, & Cifuentes, 2007;Tempels, Underberg, Somsen, & de Jong, 2007). Thus, it is possible to interface a CE instrument with a LTQ orbitrap MS using an Agilent sheath-flow adapter kit that can be used with any ESI-MS instrument.…”

Section: Using Capillary Electrophoresis To Identify the Proteome Of mentioning

confidence: 99%

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Proteomics Analysis of Kinetically Stable Proteins

Xia¹,

Manning²,

Zhang³

et al. 2012

Integrative Proteomics

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Section: Using Capillary Electrophoresis To Identify the Proteome Of supporting

confidence: 73%

Section: Using Capillary Electrophoresis To Identify the Proteome Of mentioning

confidence: 99%

Proteomics Analysis of Kinetically Stable Proteins

Xia¹,

Manning²,

Zhang³

et al. 2012

Integrative Proteomics

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“…However, as UV-absorbance detection appears to be even more challenging in chip-based microfluidics, native fluorescence utilising UV excitation below 280 nm is, besides mass spectrometric detection [18][19][20], one of the most universal detection techniques in MCE. Deep UV intrinsic fluorescence enables the detection of various analytes ranging from small aromatics to large proteins.…”

Section: Introductionmentioning

confidence: 99%

Impact of laser excitation intensity on deep UV fluorescence detection in microchip electrophoresis

2008

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A high intensity 266 nm continuous wave (cw-) laser developed for material processing was utilised as an excitation source for sensitive native fluorescence detection of unlabelled compounds in MCE. This 120 mW laser was attached via an optical fibre into a commercial epifluorescence microscope. With this MCE set-up we evaluated the impact of laser power on the S/N of aromatic compounds as well as of proteins. Compared with a previous work which used a 4 mW pulsed laser for excitation, improved S/N for small aromatics and to a lesser extent for proteins could be attained. The LOD of the system was determined down to 24 ng/mL for serotonin (113 nM), 24 ng/mL for propranolol (81 nM), 80 ng/mL for tryptophan (392 nM) and 80 ng/mL for an aromatic diol (475 nM). Sensitive protein detection was obtained at concentrations of 5 mg/mL for lysocyme, trypsinogen and chymotrypsinogen (340, 208 and 195 nM, respectively). Finally, a comparison of the cw-with a pulsed 266 nm laser, operating at the same average power, showed a higher attainable sensitivity of the cw-laser. This can be attributed to fluorescence saturation and photobleaching effects of the pulsed laser at high pulse energies.

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“…CE and LC are similar with respect to resolution and compatibility with mass spectrometers. Advantages of CE are absence of buffer gradients and speed (37). Furthermore, CE is generally insensitive towards precipitating proteins and peptides that often interfere with LC-separation, and the capillary can be reconditioned with NaOH, enabling efficient cleaning after each run.…”

Section: Capillary Electrophoresis Coupled To Mass Spectrometry (Ce-ms)mentioning

confidence: 99%

Urinary Proteome Analysis using Capillary Electrophoresis Coupled to Mass Spectrometry: A Powerful Tool in Clinical Diagnosis, Prognosis and Therapy Evaluation

Mischak¹,

Schiffer²,

Zürbig³

et al. 2009

Journal of Medical Biochemistry

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Kratak sadr`aj: Analiza proteoma je postala je mo}no sredstvo za de{ifrovanje (pato)fiziolo{kih procesa, {to je za rezultat imalo uspostavljanje oblasti klini~ke proteomike. Jedan od glavnih ciljeva je otkrivanje biomarkera oboljenja iz tkiva i telesnih te~nosti. Zbog ogromne slo`enosti pro teoma, pri proteomskoj analizi zasnovanoj na masenoj spektrometriji potrebno je izvr{iti separaciju. U radu su opisane prednosti i ograni~enja proteomske analize pri separaciji proteina putem dvodimenzionalne gel elektroforeze, te~ne hromatografije, SELDI i kapilarne elektroforeze (KE), sa fokusom na KE-MS. KE-MS omogu}ava separaciju i detekciju proteoma male molekularne te`ine u biolo{kim te~nostima uz visoku reproducibilnost i preciznost u samo jednom koraku radnog postupka i za kratko vreme. Po{to pojedina~ni senzitivni i specifi~ni biomarkeri mo`da i ne postoje, strategija za premo{}ivanje te dijagnosti~ke praznine pomera se sa detekcije pojedina~nog analita na simultanu analizu vi{e analita koji zajedno ~ine obrazac specifi~an za dato oboljenje. Takvi pristupi, me|utim, nose sa sobom dodatne izazove, koje }emo predstaviti u ovom radu. Pored izbora odgovaraju}ih tehnolo{kih platformi, neophodan je visok nivo standar dizacije proteomskih merenja i obrade podataka kako bi se vr{ilo profilisanje proteoma. U tom pogledu, zahtevi koji se ti~u nacrta studija, izbora primeraka uzoraka, analize proteomskih podataka i klini~ke evaluacije trebalo bi da budu razmotreni pre izvo|enja proteomske studije.Klju~ne re~i: klini~ka proteomika, kapilarna elektro foreza, masena spektrometrija, biomarker, urin Summary: Proteome analysis has emerged as a powerful tool to decipher (patho)physiological processes, resulting in the establishment of the field of clinical proteomics. One of the main goals is to discover biomarkers for diseases from tissues and body fluids. Due to the enormous complexity of the proteome, a separation step is required for mass spectrometry (MS)-based proteome analysis. In this review, the advantages and limitations of protein separation by two-dimensional gel electrophoresis, liquid chromatography, surface-enhanced laser desorption/ionization and capillary electrophoresis (CE) for proteomic analysis are described, focusing on CE-MS. CE-MS enables separation and detection of the small molecular weight proteome in biological fluids with high reproducibility and accuracy in one single processing step and in a short time. As sensitive and specific single biomarkers generally may not exist, a strategy to overcome this diagnostic void is shifting from single analyte detection to simultaneous analysis of multiple analytes that together form a disease-specific pattern. Such approaches, however, are accompanied with additional challenges, which we will outline in this review. Besides the choice of adequate technological platforms, a high level of standardization of proteomic measurements and data processing is also necessary to establish proteomic profiling. In this regard, demands concerning study design, choice of specimens, ...

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Trends in CE‐MS 2005–2006

Cited by 73 publications

References 187 publications

Proteomics Analysis of Kinetically Stable Proteins

Proteomics Analysis of Kinetically Stable Proteins

Impact of laser excitation intensity on deep UV fluorescence detection in microchip electrophoresis

Urinary Proteome Analysis using Capillary Electrophoresis Coupled to Mass Spectrometry: A Powerful Tool in Clinical Diagnosis, Prognosis and Therapy Evaluation

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