Absolute Myoglobin Quantitation in Serum by Combining Two-Dimensional Liquid Chromatography−Electrospray Ionization Mass Spectrometry and Novel Data Analysis Algorithms

Mayr, Bettina M.; Kohlbacher, Oliver; Reinert, Knut; Sturm, Marc; Gröpl, Clemens; Lange, Eva; Klein, Christoph; Huber, Christian G.

doi:10.1021/pr050344u

Cited by 77 publications

(53 citation statements)

References 37 publications

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“…One is through the measurement of peak intensities of peptide ions (12)(13)(14) and the other is to count the number of peptides observed for a particular protein and to compare this with the theoretical number of observable peptides (15). Non-labeled protein standards at a known concentration are added to the assay and quantified simultaneously in order to obtain absolute measurements for analyte proteins (16). MS-based absolute quantification methods have been extensively reviewed in the literature (17)(18)(19)(20)(21)(22)(23)(24).…”

Section: Introductionmentioning

confidence: 99%

Choice of LC-MS Methods for the Absolute Quantification of Drug-Metabolizing Enzymes and Transporters in Human Tissue: a Comparative Cost Analysis

Feteisi

Achour

Barber

et al. 2015

AAPS J

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Abstract. The quantification of drug-metabolizing enzymes and transporters is important for in vitro-in vivo extrapolation (IVIVE) of xenobiotic clearance, which has become an integral part of drug development. There are different mass spectrometry-based techniques used for quantitative proteomics, and as more laboratories are opting for the use of these methods, selecting the most appropriate tool is becoming a concern. For the first time, we attempt to determine the significance of cost of different LC-MS methods of quantitative analysis of these proteins and to present a framework to objectively assess the choice of the techniques. Based on our analysis, quantification using labeled internal standards is more expensive per sample but provides higher quality data than label-free quantification. Quantification using absolute quantification synthetic peptides is the approach of choice for analyzing less than nine proteins, whereas when quantifying a defined set of proteins (10-50), such as enzymes, in a reasonably large number of samples (20-100), the quantification concatemer technique is more economical, followed by label-free quantification. When analyzing proteomes or sub-proteomes (≥500 proteins), label-free quantification is more cost-effective than the use of labeled internal standards. A cost-benefit approach is described to assess the choice of the most appropriate mass spectrometrybased approach for the quantification of proteins relevant to IVIVE.

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Section: Introductionmentioning

confidence: 99%

Choice of LC-MS Methods for the Absolute Quantification of Drug-Metabolizing Enzymes and Transporters in Human Tissue: a Comparative Cost Analysis

Feteisi

Achour

Barber

et al. 2015

AAPS J

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“…Several techniques have been described in the literature for Myo quantification [24][25][26][27][28]. Electro-analytical techniques [9,19,[29][30][31][32][33] have concerned considerable attention due to its sensitive, nondestructive, and rapid electrochemical sensing method.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical biosensor based on biomimetic material for myoglobin detection

Moreira

Dutra

Noronha

et al. 2013

Electrochimica Acta

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a b s t r a c tA novel reusable molecularly imprinted polymer (MIP) assembled on a polymeric layer of carboxylated poly(vinyl chloride) (PVC COOH) for myoglobin (Myo) detection was developed. This polymer was casted on the gold working area of a screen printed electrode (Au-SPE), creating a novel disposable device relying on plastic antibodies. Electrochemical impedance spectroscopy (EIS), cyclic voltammetry (CV) and Fourier transform infrared spectroscopy (FTIR) studies confirmed the surface modification.The MIP/Au-SPE devices displayed a linear behaviour in EIS from 0.852 to 4.26 g mL −1 , of positive slope 6.50 ± 1.48 (k mL g −1 ). The limit of detection was 2.25 g mL −1 . Square wave voltammetric (SWV) assays were made in parallel and showed linear responses between 1.1 and 2.98 g mL −1 . A current decrease was observed against Myo concentration, producing average slopes of −0.28 ± 0.038 A mL g −1 . MIP/Au-SPE also showed good results in terms of selectivity. The error% found for each interfering species were 7% for troponin T (TnT), 11% for bovine serum albumin (BSA) and 2% for creatine kinase MB (CKMB), respectively. Overall, the technical modification over the Au-SPE was found a suitable approach for screening Myo in biological fluids.

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“…Defined XML schemata act as mediator, allowing multiple input formats to be subjected to a common data analysis pipeline (mzXML) [47]. Since then, several proteomics toolkits, such as OpenMS [48] or the software collection from the "Trans-Proteomic Pipeline" (http:// tools.proteomecenter.org/software.php) provide a set of computational tools for gel-free proteomics [47].…”

Section: Discussionmentioning

confidence: 99%

PROTEOMER: A workflow‐optimized laboratory information management system for 2‐D electrophoresis‐centered proteomics

Nebrich¹,

Herrmann²,

Hartl³

et al. 2009

Proteomics

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In recent years proteomics became increasingly important to functional genomics. Although a large amount of data is generated by high throughput large-scale techniques, a connection of these mostly heterogeneous data from different analytical platforms and of different experiments is limited. Data mining procedures and algorithms are often insufficient to extract meaningful results from large datasets and therefore limit the exploitation of the generated biological information. In our proteomic core facility, which almost exclusively focuses on 2-DE/MS-based proteomics, we developed a proteomic database custom tailored to our needs aiming at connecting MS protein identification information to 2-DE derived protein expression profiles. The tools developed should not only enable an automatic evaluation of single experiments, but also link multiple 2-DE experiments with MS-data on different levels and thereby helping to create a comprehensive network of our proteomics data. Therefore the key feature of our "PROTEOMER" database is its high cross-referencing capacity, enabling integration of a wide range of experimental data. To illustrate the workflow and utility of the system, two practical examples are provided to demonstrate that proper data cross-referencing can transform information into biological knowledge.

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Absolute Myoglobin Quantitation in Serum by Combining Two-Dimensional Liquid Chromatography−Electrospray Ionization Mass Spectrometry and Novel Data Analysis Algorithms

Cited by 77 publications

References 37 publications

Choice of LC-MS Methods for the Absolute Quantification of Drug-Metabolizing Enzymes and Transporters in Human Tissue: a Comparative Cost Analysis

Choice of LC-MS Methods for the Absolute Quantification of Drug-Metabolizing Enzymes and Transporters in Human Tissue: a Comparative Cost Analysis

Electrochemical biosensor based on biomimetic material for myoglobin detection

PROTEOMER: A workflow‐optimized laboratory information management system for 2‐D electrophoresis‐centered proteomics

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