Electrospray ionization Fourier transform mass spectrometry quantification of enkephalin using an internal standard

Lorenz, Sarah A.; Moy, Marie A.; Dolan, Anthony R.; Wood, Troy D.

doi:10.1002/(sici)1097-0231(19991115)13:21<2098::aid-rcm759>3.0.co;2-o

Cited by 11 publications

(2 citation statements)

References 37 publications

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“…Due to its capability in achieving high resolution and mass accuracy simultaneously, Fourier Transform Mass Spectrometry(FTMS) has gained popularity in quantitative analysis of biomolecules and biomaker discovery [1]. However, many researchers have found ion abundance accuracy of FTMS instrument problematic.…”

Section: Introductionmentioning

confidence: 99%

Processing methods for signal suppression of FTMS data

Cui

Zhang

2011

Proteome Sci

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BackgroundFourier Transform Mass Spectrometry coupled with Liquid Chromatography(LC-FTMS) has been widely used in proteomics. Past investigation has revealed that there exists an intensity dependent random suppression in peptide elution profiles in LC-FTMS data. The suppression is homogenous for the same peptide but non-homogenous for different peptides. The correction of suppressed profiles and an estimation on the range of suppression are necessary for accurate and reliable quantification using FTMS data.ResultsA software package, Gcorr, is presented. The software corrects peptide profiles that satisfy correction conditions, and it can predict fold change null distributions at different intensity levels. Subsequently, the significance P-values of measured fold changes can be estimated based on the predicted null distributions. We have used an 1:1 LC-FTMS label-free dataset pair collected based on the same sample to verify that our predicted null distributions conforms to that of the observed null distribution.ConclusionsThis software is able to provide suppression correction for peptide profiles, suppression distribution analysis and peptide differential expression analysis in terms of its fold change significance. The software is freely available at http://compgenomics.utsa.edu/Suppression_Study.html.

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Section: Introductionmentioning

confidence: 99%

Processing methods for signal suppression of FTMS data

Cui

Zhang

2011

Proteome Sci

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“…The use of internal standards for quantitation using FTICRMS was investigated by Lorenz et al 6. Methionine enkephalin was quantified using ESI coupled to a 3 T FTICR mass spectrometer, with leucine enkephalin used as the internal standard (IS).…”

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confidence: 99%

Quantitative Fourier transform ion cyclotron resonance mass spectrometry—the determination of creatinine by isotope dilution mass spectrometry

Bristow¹,

Stokes²,

O’Connor³

2005

Rapid Comm Mass Spectrometry

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Accurate quantitation has been demonstrated on many different types of mass spectrometer. However, quantitative applications of Fourier transform ion cyclotron resonance mass spectrometry (FTICRMS) have been limited. In this study, the quantitative potential of FTICRMS has been investigated using an exact matching isotope dilution method for the determination of creatinine in serum. Creatinine is an important clinical biomarker and its measurement is used as an assessment of renal function. The quantitation of creatinine was selected because a high-accuracy high-performance liquid chromatography/mass spectrometry (HPLC/MS) determination using a triple quadrupole mass spectrometer has already been successfully developed in-house. Therefore, a direct comparison of the quantitative capability of FTICRMS could be made against an established method. The accuracy of the quantitation of creatinine was found to be equivalent to that obtained using LC/MS. However, the expanded measurement uncertainty (k = 2) was larger, at 6%, when using FTICRMS compared with 1% when using HPLC/MS with the triple quadrupole mass spectrometer.

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Matrix-assisted laser desorption/ionization mass spectrometric quantification of the mu opioid receptor agonist DAMGO in ovine plasma

et al. 2000

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The synthetic opioid peptide analog Tyr-D-Ala-Gly-N-methyl-Phe-Gly-ol (DAMGO), which is a mu opioid receptor-selective agonist, was quantified in ovine plasma samples with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS), using delayed extraction and a reflectron. The internal standard was pentadeuterated DAMGO. Timed-ion selection was used to select the precursor ion. The analysis of the post-source decay fragments improved the detection sensitivity, and the use of the precursor-product ion relationship optimized the specificity. For plasma samples, the inter-assay variability of this method was 6.4% (n = 79) and the intra-assay variability was 6.0% (n = 10). The variability for controls was 3.4% (n = 43). The profile of DAMGO amount versus time was determined in sheep plasma, and the corresponding pharmacokinetic data were calculated.

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Electrospray ionization Fourier transform mass spectrometry quantification of enkephalin using an internal standard

Cited by 11 publications

References 37 publications

Processing methods for signal suppression of FTMS data

Processing methods for signal suppression of FTMS data

Quantitative Fourier transform ion cyclotron resonance mass spectrometry—the determination of creatinine by isotope dilution mass spectrometry

Matrix-assisted laser desorption/ionization mass spectrometric quantification of the mu opioid receptor agonist DAMGO in ovine plasma

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