Nanoscale packed-capillary liquid chromatography coupled with mass spectrometry using a coaxial continuous-flow fast atom bombardment interface

Moseley, M. Arthur; Deterding, Leesa J.; Tomer, Kenneth B.; Jorgenson, James W.

doi:10.1021/ac00014a023

Cited by 101 publications

(43 citation statements)

References 38 publications

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“…This matrix generally consists of an aqueous glycerol solution. The matrix solution can be either coaxially added to the post-column effluent [243,244] via an addition tee [245,246]. Alternatively, the glycerol matrix can be added to the mobile phase [247,248].…”

Section: Continuous-flow Fast Atom Bombardmentmentioning

confidence: 99%

Microcolumn liquid chromatography: instrumentation, detection and applications

Vissers¹,

Claessens

Cramers

1997

Journal of Chromatography A

208

101

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This review discusses many different aspects of microcolumn liquid chromatography (LC) and reflects the areas of microcolumn LC research interest over the past decades. A brief theoretical discussion on a number of major issues, such as column characterisation, chromatographic dilution effects and extracolumn band broadening in microcolumn LC is given. Recent progress in column technology and the demands and developments of instrumentation and accessories for microcolumn LC are also reviewed. Besides that, the developments in a large number of established and also more recent detection techniques for microcolumn LC are also discussed. The potential of hyphenation of microcolumn LC with other techniques, more particularly of multidimensional chromatography and microcolumn LC coupled to mass spectrometry is reviewed. Finally, the perspective of microcolumn LC separation methods is stressed by a number of relevant applications.

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Section: Continuous-flow Fast Atom Bombardmentmentioning

confidence: 99%

Microcolumn liquid chromatography: instrumentation, detection and applications

Vissers¹,

Claessens

Cramers

1997

Journal of Chromatography A

208

101

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“…Hence, when the valve is switched, the column effluent is blocked with excess pump flow diverting to waste through the precolumn flow splitter of the UltiMate. A 'pressure bomb' [4] was used to introduce the contents of the transfer line from Port 2 (transfer line volume set equal to the volume of a chromatographic peak at 200 nL/ min) to the mass spectrometer. The make-up solvent consisted of 0.1% formic acid in methanol/water (80:20, v/v) and was delivered to the valve at 25 nL/min.…”

Section: Variable Flow Nanoscale Lc Interfacementioning

confidence: 99%

“…T he field of protein mass spectrometry has undergone a major paradigm shift over the past several years, moving from the analysis of individual proteins to the analysis of total digests of complex protein mixtures (also know as shotgun proteomics). The development of shotgun proteomics by Yates [1-3] couples nanoscale LC for peptide analysis [4,5], automated MS to MS/MS data acquisition software and hardware on modern tandem mass spectrometers [6], along with automated database searching software of modern search engines [7,8]. Shotgun proteomics has significantly increased the information content of protein mass spectrometry experiments, while at the same time significantly reducing the total analysis time required to analyze a complex protein mixture.…”

mentioning

confidence: 99%

“…The development of shotgun proteomics by Yates [1][2][3] couples nanoscale LC for peptide analysis [4,5], automated MS to MS/MS data acquisition software and hardware on modern tandem mass spectrometers [6], along with automated database searching software of modern search engines [7,8]. Shotgun proteomics has significantly increased the information content of protein mass spectrometry experiments, while at the same time significantly reducing the total analysis time required to analyze a complex protein mixture.…”

mentioning

confidence: 99%

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A novel Interface for variable flow nanoscale LC/MS/MS for improved proteome coverage

Vissers¹,

Blackburn

Moseley

2002

J. Am. Soc. Mass Spectrom.

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A variable flow "peak trapping" liquid chromatography (LC) interface has been developed for the coupling of nanoscale LC to electrospray ionization mass spectrometry (ESI-MS). The presented peak trapping LC interface allows for the extended analysis time of co-eluting compounds and has been employed for the identification of proteins via tandem mass spectrometry (MS/MS). The variable flow process can be controlled either manually or in a completely automated manner where the mass spectrometer status determines the status of the variable flow interface. When the mass spectrometer operates in MS survey mode, the interface is operated in a so-called "high-flow" mode. Alternatively, the interface is operated in a "low-flow" mode during MS/MS analysis. In the "high-flow" mode of the variable flow process the column flow rate is typically around 200 nL/min, whereas in the "low-flow" mode the column effluent is introduced into the source of the mass spectrometer at 25 nL/min. In addition to the flow reduction during MS/MS analysis, the gradient is paused to preserve the peptide separation on the analytical nanoscale LC column. T he field of protein mass spectrometry has undergone a major paradigm shift over the past several years, moving from the analysis of individual proteins to the analysis of total digests of complex protein mixtures (also know as shotgun proteomics). The development of shotgun proteomics by Yates [1-3] couples nanoscale LC for peptide analysis [4,5], automated MS to MS/MS data acquisition software and hardware on modern tandem mass spectrometers [6], along with automated database searching software of modern search engines [7,8]. Shotgun proteomics has significantly increased the information content of protein mass spectrometry experiments, while at the same time significantly reducing the total analysis time required to analyze a complex protein mixture. Improvements in sample sensitivity and proteome coverage have been observed with this approach, compared to the "traditional" approach of using 2-D gels to separate the proteins, followed by in-gel digestion and analysis of the resulting peptides by mass spectrometry [3]. The shift in approach from the MS and MS/MS analysis of individual proteins to the analysis of complex mixtures of proteins has lead to the most significant figure of merit in proteomic analysis becoming the extent of proteome coverage obtained. Analytical methods that increase the coverage of the proteins in a sample will increase the impact of proteomics on biology.For a typical 50 kD protein, one would expect to have on the order of 40 -50 tryptic peptides. Characterization of the complex mixture of peptides resulting from a total digest of a complex protein mixture requires the mass spectrometric analysis of hundreds to many thousands of peptides. Clearly, the MS and MS/MS analysis of a sample comprised of hundreds to thousands of proteins is challenging. Modern mass spectrometers with data dependent scanning software are capable of acquiring MS and MS/MS data from many hund...

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“…The development of electrospray ionization [1], advances in miniaturized chromatography [2,3], tandem mass spectrometry (MS/MS) of peptides [4], and multidimensional liquid chromatography (LC) separations [5,6] have successively enabled other researchers in the application of mass spectrometry to their respective areas of research. As an example, we have employed the use of multidimensional LC together with automated acquisition of MS/MS data for the identification of selfpeptides and peptides originating from measles virus proteins that were displayed by the human leukocyte antigen (HLA) class II system from cultured B cells infected with measles virus [7][8][9].…”

mentioning

confidence: 99%

Accurate mass precursor ion data and tandem mass spectrometry identify a class I human leukocyte antigen A*0201-presented peptide originating from vaccinia virus

Johnson

Ovsyannikova

Madden

et al. 2005

J. Am. Soc. Mass Spectrom.

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We have used accurate mass precursor ion data generated on a hybrid linear-ion trap-Fourier transform ion cyclotron resonance mass spectrometer to augment tandem mass spectrometry (MS/MS) data generated on two different instrument types. Results from these experiments have allowed us for the first time to identify a naturally processed peptide presented by a class I human leukocyte antigen allele (HLA-A*0201) that was isolated from B cells infected by live vaccinia, the viral agent of the smallpox vaccine. The accurate mass data, in conjunction with MS/MS data, was able to identify the sequence IVIEAIHTV (aa 187-195) from the protein thymidylate kinase of vaccinia, distinguishing it from a similar sequence IVLEAIAEH: a "self-peptide" from the human protein phospholipase C␤3. Accurate mass data for the doubly charged species from the naturally processed and presented peptide was 497.8006, which was within 0.8 ppm of the calculated m/z of 497.8002, while being Ϫ37.3 ppm from the calculated m/z (497.7820) of the second-ranked peptide sequence IVLEAIAEH. Accurate mass data ranged from less than 0.1 to 1.2 ppm for other peptides identified in this sample. A BLAST search shows this sequence, IVIEAIHTV, is conserved in the same protein of a number of other orthopoxviruses, including the variola (smallpox) virus. Additionally, accurate mass data were able to uncover a false positive search result that was not distinguished by scoring of the match to the MS/MS data. [5,6] have successively enabled other researchers in the application of mass spectrometry to their respective areas of research. As an example, we have employed the use of multidimensional LC together with automated acquisition of MS/MS data for the identification of selfpeptides and peptides originating from measles virus proteins that were displayed by the human leukocyte antigen (HLA) class II system from cultured B cells infected with measles virus [7][8][9].Recently, the development and commercialization of hybrid mass spectrometers incorporating Fourier transform ion cyclotron resonance (FTICR) analyzers, with high resolving power (RP) and high mass accuracy offer additional opportunities to enhance the usefulness of

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Nanoscale packed-capillary liquid chromatography coupled with mass spectrometry using a coaxial continuous-flow fast atom bombardment interface

Cited by 101 publications

References 38 publications

Microcolumn liquid chromatography: instrumentation, detection and applications

Microcolumn liquid chromatography: instrumentation, detection and applications

A novel Interface for variable flow nanoscale LC/MS/MS for improved proteome coverage

Accurate mass precursor ion data and tandem mass spectrometry identify a class I human leukocyte antigen A*0201-presented peptide originating from vaccinia virus

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