Isotope dilution--mass spectrometric quantification of specific proteins: model application with apolipoprotein A-I

Barr, John R.; Maggio, Vincent L.; Patterson, Donald G.; Cooper, Gerald R.; Henderson, L. Omar; Turner, Wayman E.; Smith, Steven J.; Hannon, W. Harry; Ll, Needham; Sampson, Eric J.

doi:10.1093/clinchem/42.10.1676

Cited by 326 publications

(95 citation statements)

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“…Quantitative MS has become a widely applied analytical concept featuring a broad variety of data acquisition schemes. In this article, we focus on fragment ion based quantification methods ranging from classical SRM [4][5][6][7][8][9][10] to targeted MS2 (PRM/t-MS2) [11,12], sequential window acquisition of all theoretical spectra (SWATH-MS) and data independent acquisition (DIA) [13][14][15][16]. In order to simplify this manuscript targeted MS2 (PRM/t-MS2) will be abbreviated PRM and DIA modes (SWATH-MS/DIA) will be abbreviated DIA.…”

Section: Introductionmentioning

confidence: 99%

Targeted proteomics coming of age – SRM, PRM and DIA performance evaluated from a core facility perspective

et al. 2016

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Quantitative mass spectrometry is a rapidly evolving methodology applied in a large number of omics-type research projects. During the past years, new designs of mass spectrometers have been developed and launched as commercial systems while in parallel new data acquisition schemes and data analysis paradigms have been introduced. Core facilities provide access to such technologies, but also actively support the researchers in finding and applying the best-suited analytical approach. In order to implement a solid fundament for this decision making process, core facilities need to constantly compare and benchmark the various approaches. In this article we compare the quantitative accuracy and precision of current state of the art targeted proteomics approaches single reaction monitoring (SRM), parallel reaction monitoring (PRM) and data independent acquisition (DIA) across multiple liquid chromatography mass spectrometry (LC-MS) platforms, using a readily available commercial standard sample. All workflows are able to reproducibly generate accurate quantitative data. However, SRM and PRM workflows show higher accuracy and precision compared to DIA approaches, especially when analyzing low concentrated analytes.

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Section: Introductionmentioning

confidence: 99%

Targeted proteomics coming of age – SRM, PRM and DIA performance evaluated from a core facility perspective

et al. 2016

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“…In addition, samples can also be analyzed after enzymatic digestion. In this case, stable isotopelabeled peptide was used as internal standards for LC-MS/MS quantification (Anderson et al, 2004;Barnidge et al, 2004;Barr et al, 1996;Hagman et al, 2008;van den Broek et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Qualification and application of a liquid chromatography–quadrupole time‐of‐flight mass spectrometric method for the determination of trastuzumab in rat plasma

Park

Lee

Shin

2015

Biomedical Chromatography

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An liquid chromatography-quadrupole time-of-flight (QqTOF) mass spectrometric method was developed for the determination of humanized or human monoclonal antibodies in rat plasma at the early drug discovery stage. Trastuzumab was used as a model monoclonal antibody. The method consisted of immunoprecipitation followed by tryptic digestion for sample preparation and LC-TOF-MS/MS analysis of specific signature peptides in the positive ion mode using electrospray ionization for analysis. A stable isotope-labeled signature peptide was also used as internal standard. A quadratic regression (weighted 1/concentration(2) ), with an equation y = ax(2) + bx + c, was used to fit calibration curves over the concentration range of 0.500-100 µg/mL for trastuzumab. Samples from a pharmacokinetic study in rat were analyzed by this qualified LC-TOF-MS/MS method and concentrations were compared with those generated by enzyme linked immunosorbent assays method. The LC-TOF-MS/MS method was accurate and precise, with quantitative results comparable with those of ELISA. The qualification run met the acceptance criteria of ±25% accuracy and precision values for quality control samples. Within-run accuracy ranged from 1.53 to 9.20% with precision values ≤10.29%. This LC-TOF-MS/MS method approach could be used as a complementary method for humanized or human monoclonal antibodies at the early drug discovery stage.

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“…targeted proteomics methods [1]. The concept of MS-based protein quantification by MRM has been developed during the last years [2][3][4][5][6][7][8]. In general, the complex protein matrix is enzymatically digested with proteases such as trypsin to yield unique proteotypic peptides that are specific for the target proteins and can easily be separated and detected by MS [9].…”

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confidence: 99%

Quantification of seven apolipoproteins in human plasma by proteotypic peptides using fast LC‐MS/MS

Ceglarek

Dittrich

Becker

et al. 2013

Proteomics Clinical Apps

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Isotope dilution--mass spectrometric quantification of specific proteins: model application with apolipoprotein A-I

Cited by 326 publications

References 0 publications

Targeted proteomics coming of age – SRM, PRM and DIA performance evaluated from a core facility perspective

Targeted proteomics coming of age – SRM, PRM and DIA performance evaluated from a core facility perspective

Qualification and application of a liquid chromatography–quadrupole time‐of‐flight mass spectrometric method for the determination of trastuzumab in rat plasma

Quantification of seven apolipoproteins in human plasma by proteotypic peptides using fast LC‐MS/MS

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