Reverse‐phase liquid chromatography/electrospray‐ionization Fourier‐transform mass spectrometry in the analysis of peptides

Stacey, Catherine; Kruppa, Gary; Watson, Clifford H.; Wronka, John; Laukien, Frank H.; Banks, J. Fred; Whitehouse, Craig M.; Voyksner, Robert D.

doi:10.1002/rcm.1290080704

Cited by 29 publications

(9 citation statements)

References 13 publications

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“…The coupling of reversed-phase liquid chromatography with ESI-FTMS has shown reproducibility of replicate analyses and the power of broadband analysis of a gradient separation of peptides (Stacey et al, 1994). Recently, high pressure liquid chromatography (HPLC) has been combined with ESI-FTMS to enable the structural analysis of trace impurities in a drug substance (Haskins et al, 1995).…”

Section: Hyphenated Techniquesmentioning

confidence: 99%

Fourier transform mass spectrometry—advancing years (1992-mid. 1996)

Dienes

Pastor

Schürch

et al. 1996

Mass Spectrom. Rev.

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This article is one of a series of Fourier transform mass spectrometry (FTMS) reviews that has appeared in this journal at ca. 3–4 year intervals. A comprehensive review of the recent theoretical developments, instrumental developments, electrospray ionization (ESI), and MALDI is given. Ion dissociation techniques are also discussed because of their contributions to gaining insight into chemical structure. Special sections have been devoted to discussing the emerging fields of surface analysis, polymer analysis, Buckminsterfullerenes (buckyballs), and hydrogen/deuterium exchange studies. This review, although not all‐inclusive, is intended to be a starting point for those wishing to learn more about the current status of FTMS, and also as a representative cross‐section of the literature for those familiar with the technique. © 1997 John Wiley & Sons, Inc.

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Section: Hyphenated Techniquesmentioning

confidence: 99%

Fourier transform mass spectrometry—advancing years (1992-mid. 1996)

Dienes

Pastor

Schürch

et al. 1996

Mass Spectrom. Rev.

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“…Proteins separated by electrophoresis or chromatography in one or more dimensions are commonly digested off-line by a proteolytic enzyme such as trypsin and the fragment peptides analyzed by matrix assisted laser desorption/ionization (MALDI) or electrospray ionization (ESI) time-of-flight (TOF) or ion trap (IT) mass spectrometry [1,2]. Capillary electrophoresis (CE) MS [3,4] or liquid chromatography (LC) MS [5][6][7] coupled to mass spectrometry through ESI have been used to identify proteins in complex biological samples such as whole cell lysates [4,[8][9][10][11] and human body fluids [12][13][14]. The main purpose of combining a liquid separation method with an electrospray mass spectrometer is to reduce the complexity of sample introduced to the mass spectrometer at any given time, resulting in an enhanced dynamic (concentration) range.…”

Section: Introductionmentioning

confidence: 99%

Protein identification by liquid chromatography–mass spectrometry using retention time prediction

Palmblad

Ramström

Bailey

et al. 2004

Journal of Chromatography B

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“…To fully establish ESI-FTICR-MS as a practical quantitative tool, there is much interest in coupling on-line separation techniques such as high performance liquid chromatography 17 and capillary electrophoresis [18][19][20][21] to the electrospray source. In order to maintain the resolution of the on-line separation, rapid acquisition of spectra is required; thus, it becomes imperative that sampling, ionization, and excitation and detection of the image current occurs in as short a time as possible.…”

mentioning

confidence: 99%

Quantification of singly charged biomolecules by electrospray ionization fourier transform ion cyclotron resonance mass spectrometry utilizing an internal standard

Gordon

Muddiman

1999

Rapid Commun. Mass Spectrom.

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The quantification of Cyclosporin A (CsA) and related biological compounds by various mass spectrometric techniques is well established. It is precisely this fact that makes the use of CsA particularly appealing as a model system in evaluating the quantitative properties of electrospray ionization coupled to Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR-MS). Utilizing the internal standard methodology, we have generated a linear calibration curve ranging from 5-250 ng/mL CsA described by the equation y = 0.00503x-0.00958, with a %RSD slope of 0.74% and a correlation coefficient (r 0 ) equal to 0.999 2 (N = 30). The internal standard (200 ng/mL Cyclosporin G) was found to be necessary to establish the reported dynamic range, two orders of magnitude based on an experimentally determined detection limit of 2.4 ng/mL CsA, and also significantly improved the overall precision of the method. The data represented in the standard curve were collected as 1.05 s single acquisitions (512 K data points at an ADC rate of 500 kHz) and unapodized prior to the Fourier transformation of the time-domain data. We report that full Hanning apodization has a statistically significant negative effect (F-test at 95% confidence level) on the regression statistics of the curve (i.e. increasing the %RSD slope to 1.33%). Finally, we report that acceptable quantitative properties of an FTICR-MS experiment can be realized as soon as the detection of a second isotopic beat for the targeted species is obtained. This should allow for the practical and effective coupling of on-line separation techniques for quantitative analysis using ESI-FTICR-MS. Copyright # 1999 John Wiley & Sons, Ltd. Received 4 December 1998; Accepted 4 December 1998Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) has been demonstrated to have impressive capabilities for the analytical characterization of biological materials. Recent reports have described such varied investigations as highly accurate molecular mass determinations of peptides and proteins, 1-4 high resolution tandem mass spectra of exceedingly large biomolecules (b10 kDa), 2,5,6 and structural verification of 50-to 100-mer DNA and RNA sequences. 7,8 The maturation of this increasingly useful technique in the qualitative analysis of biological compounds is well documented. Interestingly, one area of research that has been comparatively slow to develop is the exploration of electrospray ionization (ESI) FTICR-MS as a quantitative tool. Limbach et al. reported the first experimental demonstration of the potentially achievable detection limit ($177 ions at S/N = 3) and dynamic range (b4 orders of magnitude) for an FTICR mass spectrometer with a 1.875-in cubic trap housed within a 3.0 T superconducting magnet. 9 In a more empirical approach, Padley and co-workers quantified both singly and multiply charged ions according to their absolute peak intensities 10 utilizing ESI and observed linearity of $2-3 orders of magnitude for singly charged lysine (147 Da) and 1.5 or...

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Reverse‐phase liquid chromatography/electrospray‐ionization Fourier‐transform mass spectrometry in the analysis of peptides

Cited by 29 publications

References 13 publications

Fourier transform mass spectrometry—advancing years (1992-mid. 1996)

Fourier transform mass spectrometry—advancing years (1992-mid. 1996)

Protein identification by liquid chromatography–mass spectrometry using retention time prediction

Quantification of singly charged biomolecules by electrospray ionization fourier transform ion cyclotron resonance mass spectrometry utilizing an internal standard

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