Improved electrospray ionization interface for capillary zone electrophoresis-mass spectrometry

Smith, Richard D.; Barinaga, Charles J.; Udseth, Harold R.

doi:10.1021/ac00169a022

Cited by 540 publications

(296 citation statements)

References 8 publications

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“…ESI is the method of choice for producing gas phase ions from solution because it is a very soft ionization method and is useful for the ionization of larger molecules or biomolecules. ESI-MS can be used for the analysis of complex mixtures [1][2][3][4][5] and is commonly used to couple separation techniques, such as high performance liquid chromatography (HPLC) [6][7][8][9], capillary electrophoresis (CE) [10][11][12][13][14][15][16][17][18][19][20][21], or microchannel electrophoresis (ME) [22][23][24][25][26][27][28][29] with MS. Many sample introduction methods, particularly those that employ separations, rely on pressure driven flow for sample introduction.…”

Section: Introductionmentioning

confidence: 99%

A Study of Electrospray Ionization Emitters with Differing Geometries with Respect to Flow Rate and Electrospray Voltage

Reschke

Timperman

2011

J. Am. Soc. Mass Spectrom.

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The performance of several electrospray ionization emitters with different orifice inside diameters (i.d.s), geometries, and materials are compared. The sample solution is delivered by pressure driven flow, and the electrospray ionization voltage and flow rate are varied systematically for each emitter investigated, while the signal intensity of a standard is measured. The emitters investigated include a series of emitters with a tapered outside diameters (o.d.) and unaltered i.d.s, a series of emitters with tapered o.d.s and i.d.s, an emitter with a monolithic frit and a tapered o.d., and an emitter fabricated from polypropylene. The results show that for the externally etched emitters, signal was nearly independent of i.d. and better ion utilization was achieved at lower flow rates. Furthermore, emitters with a 50 μm i.d. and an etched o.d. produced about 1.5 times more signal than etched emitters with smaller i.d.s and about 3.5 times more signal than emitters with tapered inner and outer dimensions. Additionally, the work presented here has important implications for applications in which maximizing signal intensity and reducing frictional resistance to flow are necessary. Overall, the work provides an initial assessment of the critical parameters that contribute to maximizing the signal for electrospray ionization sources interfaced with pressure driven flows.

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Section: Introductionmentioning

confidence: 99%

A Study of Electrospray Ionization Emitters with Differing Geometries with Respect to Flow Rate and Electrospray Voltage

Reschke

Timperman

2011

J. Am. Soc. Mass Spectrom.

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“…T he two dominant separation methods used in proteomics are 2-dimensional gel electrophoresis [1] and, increasingly, liquid chromatography (LC) [2]. The first use of LC to obtain sequence information from proteins was by Fredrick Sanger in the 1940s and LC separation methods have experienced rapidly growing use since online LC-MS analysis based upon electrospray ionization (ESI) was demonstrated in the early 1990s [3][4][5][6][7]. Although most early efforts were used for analysis of peptides from digests of nominally isolated proteins, of most interest currently are methods that can be used to analyze as many as hundreds of thousands of separate species from a single organism or sample with high reproducibility from run-to-run.…”

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confidence: 99%

Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry

Strittmatter

Ferguson

Tang

et al. 2003

J. Am. Soc. Mass Spectrom.

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We describe the application of capillary liquid chromatography (LC) time-of-flight (TOF) mass spectrometric instrumentation for the rapid characterization of microbial proteomes. Previously (Lipton et al., Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 11049) the peptides from a series of growth conditions of Deinococcus radiodurans have been characterized using capillary LC MS/MS and accurate mass measurements which are captured as an accurate mass and time (AMT) tag database. Using this AMT tag database, detected peptides can be assigned using measurements obtained on a TOF due to the additional use of elution time data as a constraint. When peptide matches are obtained using AMT tags (i.e., using both constraints) unique matches of a mass spectral peak occurs 88% of the time. Not only are AMT tag matches unique in most cases, the coverage of the proteome is high; ϳ3500 unique peptide AMT tags are found on average per capillary LC run. From the results of the AMT tag database search, ϳ900 ORFs detected using LC-TOFMS, with ϳ500 ORFs covered by at least two AMT tags. These results indicate that AMT database searches with modest mass and elution time criteria can provide proteomic information for approximately one thousand proteins in a single run of Ͻ3 h. The advantage of this method over using MS/MS based techniques is the large number of identifications that occur in a single experiment as well as the basis for improved quantitation. For MS/MS experiments, the number of peptide identifications is severely restricted because of the time required to dissociate the peptides individually. These results demonstrate the utility of the AMT tag approach using capillary LC-TOF MS instruments, and also show that AMT tags developed using other instrumentation can be effectively utilized. (J Am Soc Mass Spectrom 2003, 14, 980 -991)

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“…[19] This system allows for the stable formation of ions in the MS system; however, its disadvantage is that the auxiliary liquid dilutes the sample. [20,21] …”

Section: Coaxial Sheath Liquid Flowmentioning

confidence: 99%

Homemade Capillary Electrophoresis Coupled to a Mass Spectrometer

Moraes

Carrilho

Assunção

2014

Journal of Liquid Chromatography & Related Technologies

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A system was developed in our laboratory to couple capillary electrophoresis with mass spectrometry. The capillary electrophoresis system was equipped with a high voltage supply, and a microcontroller with assembly language programming was developed for the computational control of the system. The MS system was a commercial Thermo Finningan LCQ ion trap mass spectrometer. The robustness of the coupled system was evaluated using standard protein samples (lysozyme, aprotinin, and bovine albumin) and tryptic digests of lysozyme. The system showed positive results in terms of robustness, allowing for the separation of digested proteins and the identification of 33% of the total amino acids in a protein (6 of the 18 expected peptides). The limit of detection was in the order of 1 picomole (signal-to-noise ratio), which was considered satisfactory for this system. The system shows high versatility in tandem coupling and combinations with other analytical procedures.

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Improved electrospray ionization interface for capillary zone electrophoresis-mass spectrometry

Cited by 540 publications

References 8 publications

A Study of Electrospray Ionization Emitters with Differing Geometries with Respect to Flow Rate and Electrospray Voltage

A Study of Electrospray Ionization Emitters with Differing Geometries with Respect to Flow Rate and Electrospray Voltage

Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry

Homemade Capillary Electrophoresis Coupled to a Mass Spectrometer

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