Quantitative mass spectrometry

Ensure Precise Structural Characterization and Quantification Of Complex Biologics. Download Our White Paper On HCP Analysis Quantitative mass spectrometry: an overview. Mass spectrometry (MS) is a mainstream chemical analysis technique in the twenty-first century. It has contributed to numerous discoveries in chemistry, physics and biochemistry. Hundreds of research laboratories scattered all over the world use MS every day to investigate fundamental phenomena on t This article is part of the themed issue 'Quantitative mass spectrometry'. Mass spectrometry (MS) is commonly regarded as an instrumental technique for separation of electrically charged species in the gas phase (for general information, see for example [ 1 - 11 ]). The charged species (ions) are produced in the ion source The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained.

Quantitative mass spectrometry-based proteomics is now being applied on a large scale to address interesting biological questions. The 'SILAC mouse': metabolic isotope labeling now allows.. Quantitative pharmaceutical analysis is nowadays frequently executed using mass spectrometry. Electrospray ionization coupled to a (hybrid) triple quadrupole mass spectrometer is generally used in combination with solid-phase extraction and liquid chromatography Quantitative Mass Spectrometry-based Proteomics 1. Introduction. Analysis of the proteome using mass spectrometry has proven to be an indispensable tool in biomedical... 2. Mass spectrometry-based proteomics. Before the application of mass spectrometry, protein analysis was mostly based on... 3..

The Quantitative Mass Spectrometry Imaging (QMSI) is a technique developed for: the detection target molecules (drugs, metabolites, lipids, endogenous metabolites, peptides and proteins) or elements (Zinc, Copper, Gold, Calcium, Iron, Gadolinium, etc.) A quantitative mass spectrometry-based approach to monitor the dynamics of endogenous chromatin-associated protein complexe Quantitative mass spectrometry. Quantitative proteomics is an analytical chemistry technique for determining the amount of proteins in a sample. [1] [2] [3] The methods for protein identification are identical to those used in general (i.e. qualitative) proteomics , but include quantification as an additional dimension You can safely state that mass spectrometry is quantitiative between the same peptide / phosphopeptide overall protein all treated under same conditions, for multiple experiments. Eg., time course,..

The basic principle in quantitative analysis by mass spectrometry is the measurement of a signal representative of the mass of the analyte relative to a known amount of an internal mass standard Quantitative analysis of mass spectrometry proteomics data - software for improved life science Abstract: The rapid advances in life science, including the sequencing of the human genome and numerous other techiques, has given an extraordinary ability to aquire data on biological systems and human disease. Eve Quantitative Mass Spectrometry. Multiple methods allow for the quantitation of proteins by mass spectrometry ( quantitative proteomics ), [15] and recent advances have enabled quantifying thousands of proteins in single cells

Quantitative live cell mass spectrometry analysis at a subcellular level requires the precisely controlled extraction of subpicoliter volumes of material from the cell, sensitive analysis of the extracted analytes, and their accurate quantification without prior separation. In this study, we demonstrate that localized electroosmotic extraction provides a direct path to addressing this. Mass spectrometry (MS)-based assays have unique advantages: e.g., high specificity, wide dynamic range, fast method development, and ability to quantify multiple proteins simultaneously. As a result, MS-based assays have been gaining increasing attention and interest for the quantitative bioanalysis of proteins in recent years [ 3 - 14 ]

Matrix interferences can be overcome in a variety of ways, including sample cleanup, or using internal standard Mass spectrometry (MS) has been a core technology for high sensitive and high‐throughput analysis of the enriched glycoproteome in aspects of quantitative assays as well as qualitative profiling of glycoproteins Quantitative mass spectrometry revealed the identification of numerous differentially regulated proteins over three days of postnatal development. These data provide insights into functional pathways regulating normal sensory and supporting cell development in the cochlea that include potential biomarkers

Covalent labeling with mass spectrometry (CL-MS) provides a direct measure of the chemical and structural features of proteins with the potential for resolution at the amino-acid level. Unfortunately, most applications of CL-MS are limited to narrowly defined differential analyses, where small numbers of residues are compared between two or more protein states MSstats: an R package for statistical analysis of quantitative mass spectrometry-based proteomic experiments Bioinformatics , 30 ( 2014 ) , pp. 2524 - 2526 , 10.1093/bioinformatics/btu305 Google Schola In this study, we integrated technological advancements in quantitative mass spectrometry (MS) (9 - 11), including labeling multicellular organisms with the 15 N stable isotope, to identify DAF-2..

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Fluid diagnostics analysis - The next-gen spectromete

  1. Traditional instrumentation used for quantitative bioanalysis in industry, such as reverse phase liquid chromatography and SRM (QqQ) mass spectrometry, while considered highly selective, and therefore well suited for bottom-up techniques, is not generally effective with regards to intact quantification
  2. An introduction to the basic principles for quantitative mass-spectrometry analysis of proteins. Learn more about this class http://slavovlab.net/teaching/in..
  3. Quantitative mass spectrometry imaging of small-molecule neurotransmitters in rat brain tissue sections using nanospray desorption electrospray ionization H. Bergman, E. Lundin, M. Andersson and I. Lanekoff, Analyst, 2016, 141, 3686 DOI.

Quantitative Applications of Mass Spectrometry I. Lavagnini, F. Magno, R. Seraglia and P. Traldi # 2006 John Wiley & Sons, Ltd method to be employed is addressed by the physico-chemical propertie When developing new medicines, pharmaceutical companies, contract research organisations (CROs) and academic laboratories need to quantify exactly how much of a drug or its metabolites are present in the fluid or tissue of a biological system Qualitative and Quantitative Analysis of Impurities, including Host Cell Proteins (HCPs), using Mass Spectrometry. The processes involved in producing and purifying a biopharmaceutical use many different chemicals and reagents which can result in low-levels of residual impurities in the final Active Pharmaceutical Ingredient (API) Andrey Tarasov, Manual quantitative gas analysis; Mass-spectrometry 4 1. General considerations. 5 - Assess costs and time for the calibration (expenses and delivery time of gas mixtures, additional valves, gas tube connections, heaters, pumps, saturator, pressure reducer) Mass Spectrometry Uses MS is used for both qualitative and quantitative chemical analysis. It may be used to identify the elements and isotopes of a sample, to determine the masses of molecules, and as a tool to help identify chemical structures. It can measure sample purity and molar mass

Qualitative and Quantitative Host Cell Protein Analysis Using Mass Spectrometry View PDF by Jillian Roamer and Victor Sharov Thursday, February 14, 2019 12:54 p Quantitative mass spectrometry of proteins has evolved dramatically over the last decade. Early methods involved labeling proteins with reagents enriched in stable isotopes in order to introduce mass tags into proteins of interest for relative quantification of proteins [ 1, Mass spectrometry-based label-free quantitative proteomics falls into two general categories. In the first are the measurements of changes in chromatographic ion intensity such as peptide peak areas or peak heights. The second is based on the spectral counting of identified proteins Mass spectrometry (MS) has become the de facto tool for routine quantitative analysis of biomolecules. MS is increasingly being used to reveal the spatial distribution of proteins, metabolites, and pharmaceuticals in tissue and interest in this area has led to a number of novel spatially resolved MS technologies

Advanced Analytics for Improved Biologic Developmen

Leader In HCP Analysis - LC-MS Based Profilin

  1. An automated continuous reactor for the synthesis of organic compounds, which uses online mass spectrometry (MS) for reaction monitoring and product quantification, is presented. Quantitative and rapid MS monitoring was developed and calibrated using HPLC. The amidation of methyl nicotinate with aqueous MeN
  2. Trace Quantitative Analysis by Mass Spectrometry is a wonderful book for beginner and intermediate students, analysts, and scientists keen on learning more about mass spectrometry. The authors' discussion of history and the evolution of relevant science make the text lively and engaging, no small achievement for a book about analytical science
  3. Pris: 1009 kr. Inbunden, 2008. Skickas inom 7-10 vardagar. Köp Trace Quantitative Analysis by Mass Spectrometry av Robert K Boyd, Cecilia Basic, Robert A Bethem på Bokus.com

Tissue Extracts for Quantitative Mass Spectrometry of Planarian Proteins Using SILAC Alexander Böser, Hannes C. A. Drexler, and Kerstin Bartscherer Abstract SILAC (stable isotope labeling by amino acids in cell culture) proteomics enables the relative quantification of proteins in one or more biological samples by mass spectrometry Mass spectrometry is used for both qualitative and quantitative study of chemical substances. These can be used to classify a sample's elements and isotopes, to determine molecular masses, and as a tool for helping to classify chemical structures. This can calculate the purity of the samples and the molar mass Although MSI as a field has existed for more than 20 years, quantitative mass spectrometry imaging (qMSI) is still in its infancy, and unlike in traditional bioanalysis employing HPLC-MS, there is not yet an established consensus on how to construct calibration curves and assess tissue concentrations This article is part of the themed issue 'Quantitative mass spectrometry'. Keywords: clinical analysis, toxicology, hyphenated techniques, mass spectrometry, non-invasive sampling 1. Introduction Unconventional biological matrices have recently attracted much attention. They are perceived as 1 1,2 1

Quantitative mass spectrometry: an overvie

With less sample than western blotting and no antibodies needed, modern quantitative mass spectrometry analyses can detect and quantify thousands of proteins in a single experiment across multiple conditions, and the dynamics can be studied at a level that provides much greater understanding of how biological processes respond to different stimuli, or how they change within a cell, tissue, or organism over time, or while in a disease state A quantitative mass spectrometry imaging (QMSI) method for absolute quantification of glutathione (GSH) in healthy and cancerous hen ovarian tissues using infrared matrix-assisted laser desorption. quantitative mass spectrometry-based proteomics. We focus on class comparison using Analysis of Variance (ANOVA), and discuss how randomization, replication and blocking help avoid systematic biases due to the experimental procedure, and help optimize our ability to detect true quantitative changes between groups Quantitative features for mass spectrometry data Evolving MSnSet data towards SummarizedExperiment, but for MS data. QFeatures is a Bioconductor package that provides infrastructure enabling the management and processing of quantitative features for high-throughput mass spectrometry assays

CFMP - Methods -> Quantitative Proteomics

Quantitative mass spectrometry: an overview

Mass spectrometry (MS) is a powerful analytical tool with many applications in pharmaceutical and biomedical field. The increase in sensitivity and resolution of the instrument has opened new dimensions in analysis of pharmaceuticals and complex metabolites of biological systems. Compared with other techniques, mass spectroscopy is only the technique for molecular weight determination, through. Quantitative mass spectrometry imaging (MSI) is an effective technique for determining the spatial distribution of molecules in a variety of sample types; however, the quality of the ion signals is related to the chemical and morphological properties of the tissue and the targeted analyte (s) In this short Review, with 2 tables, 2 figures, and 31 references, we highlight how mass spectrometry analysis can be used to quantitatively study the proteome. In particular, we describe challenges to analyzing posttranslational modifications of proteins, which serve to transduce information through signaling pathways that control cellular behavior

Quantitative mass spectrometry in proteomics: a critical

Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research. Correction(s) for this article Sebastian Wiese. Medizinisches Proteom‐Center, Ruhr‐Universität Bochum, Bochum, Germany. Search for more papers by this author. Kai A. Reidegeld. Quantitative features for mass spectrometry data. Evolving MSnSet data towards SummarizedExperiment, but for MS data. New classes to manage and process quantitative features for high-throughput mass spectrometry assays. See the QFeatures homepage for details LC coupled with MS and tandem mass spectrometry (MS n) is being adopted in a number of hospital laboratories for the quantitative analysis of a number of analytes from physiological matrices, but standards for development and validation of such assays are not easily available

Quantitative mass spectrometry-based proteomics is a technology of growing importance in biological and clinical research Thank you for sending your work entitled A combined quantitative mass spectrometry and electron microscopy analysis of ribosomal 30S subunit assembly in E. coli for consideration at eLife. Your article has been favorably evaluated by James Manley (Senior editor), a Reviewing Editor, and two other reviewers, both of whom, Harry Noller and Peter Moore, have agreed to reveal their identity MassHunter Qualitative Analysis is mass spec screening software for the confirmation of target or suspect compounds, and for the identification of unknown analytes. Mass spec identification analysis is supported by advanced data mining, processing, and reporting options that let you rapidly and accurately find and confirm target/suspect compounds and easily identify unknowns Current Status and Advances in Quantitative Proteomic Mass Spectrometry ValerieC.Wasinger, 1 MingZeng, 1 andYunkiYau 1,2 Bioanalytical Mass Spectrometry Facility, Mark Wainwright Analytical Centre, e University of New South Wales, Sydney,NSW,A ustrali

Mass spectrometry quantitative analysis software for routine, high-throughput, and profiling workflows. MassHunter Quantitative Analysis software supports sensitive mass spec quantitation of known and suspect compounds in pharmaceutical, food, environmental, energy, and forensic toxicology testing applications Identification of psoriatic arthritis mediators in synovial fluid by quantitative mass spectrometry. Daniela Cretu 1,2, Ioannis Prassas 1,2, Punit Saraon 1,2, Ihor Batruch 2, Rajiv Gandhi 3,4, Eleftherios P Diamandis 1,2,5 & Vinod Chandran 3,6,7 Clinical Proteomics volume 11, Article number: 27 (2014) Cite this articl The basic principle in quantitative analysis by mass spectrometry is the measurement of a signal representative of the mass of the analyte relative to a known amount of an internal mass standard. To ensure that the signal is representative of the particular substance to be measured and not a result of some other substance in the biological matrix, a range of analytical methods have been employed The Mass Spectrometry Unit at Stellenbosch University in the Western Cape performs quantitative and qualitative analysis of organic molecules using Mass spectrometry. Services include GC-MS analysis, LC-MS analysis, accurate mass determinations and Proteomic analysis Lipid droplets are important organelles for the replication of several pathogens, including the Hepatitis C Virus (HCV). We describe a method to isolate lipid droplets for quantitative mass spectrometry of associated proteins; it can be used under a variety of conditions, such as virus infection, environmental stress, or drug treatment

While initial proteomic studies were limited by the status of mass spectrometry (MS) technology (Bull and Thiede, 2012; Mintz et al., 2008), a more recent proteomic study used a recombinant system to uncover the direct targets of XBP1 and ATF6, purposefully excluding the effects of ER stress, IRE1 and PERK activation, as wells as ATF4 and CHOP expression (Shoulders et al., 2013) Liquid chromatography-mass spectrometry (LC-MS)-based quantitative proteomics has become increasingly applied for a broad range of biological applications due to growing capabilities for broad proteome coverage and good accuracy in quantification. Herein, we review the current LC-MS-based. Mass spectrometry: hypothesis-free protein detection is affected by high abundance proteins and peptide ionization. Both high throughput technologies are capable of semi-quantitative and quantitative data. Antibody arrays and mass spectrometry complement each other

GC/MS - MooreAnalytical

Since mass spectrometry is not inherently quantitative, most methods rely on the introduction of stable isotopes in the specific pull-down and the control. This allows a pair-wise, quantitative comparison of peptides between the two samples and enables discrimination of highly abundant background proteins from specific interactors ( 3 ) Mass spectrometry for real-time quantitative breath analysis David Smith1,5, Patrik Spanˇ elˇ 2, Jens Herbig3 and Jonathan Beauchamp4 1 Institute for Science and Technology in Medicine, Keele University, Guy Hilton Research Centre, Thornburrow Drive, Stoke-on-Trent ST4 7QB, U To maximize quantitative accuracy and precision, synchronous precursor selection (SPS)-based MS 3 technology is used, developed by Gygi Lab. The facility utilizes an Orbitrap Eclipse™ Tribrid™ Mass Spectrometer coupled with a Liquid Chromatography System (EASY-nLC™ 1200 System) and a wet lab

Mass spectrometry-based proteomics methodology has become an important tool in elucidating some of the underlying mechanisms involved in cardiovascular disease. The present review provides details on selected important protein targets where highly selective and specific mass spectrometry-based approaches have led to important new findings and provided new mechanistic information 2. Mass spectrometry data acquisition. Preparation of muropeptides for mass spectrometry. Supplement 800 μg of purified sacculi with 100 μg/mL mutanolysin, 100 mM ammonium acetate pH 5.5, and 50 mM magnesium chloride in a 100 μL reaction. Digest at 37 °C overnight The accepted way of performing mass spec quantitation is by using a mass spectrometer capable of MS/MS fragmentation. MS/MS used in conjunction with quantitation is commonly accomplished with a triple quadrupole or ion trap mass spectrometer

Quantitative mass spectrometry Nature Method

De Leenheer, Andreas, and Linda Thienpont. Quantitative Mass Spectrometry. Advances in Mass Spectrometry. Eds. P. Kistemaker, N. Nibbering, Elsevier, Amsterdam. Huang et al. 1 have recently developed a quantitative mass spectrometry-based assay for identifying protein kinase substrates and quantifying kinase activity. This approach offers several advantages over current methods: It is label-free and eliminates the need for fluorescent or radiolabel detection of phosphorylated substrate In order to quantify the larger number of proteins, two different quantitative methods were applied: spectral count and TMT isobaric labeling. The quantitative PAcIFIC technology proved to be a powerful tool for the discovery of proteins differentially abundant between pooled plasma samples from AAA and control patients

Mass spectrometry (MS)-based proteomics is the most comprehensive approach for the quantitative profiling of proteins, their interactions and modifications. It is a challenging topic as a firm grasp requires expertise in biochemistry for sample preparation, analytical chemistry for instrumentation and computational biology for data analysis Mass Spectrometry is important Chemical analysis method. Mass Spectrometry is a various application in the field of chemistry and pharmaceutics. In pharmaceutical Industry and drug analysis and Mass Spectrometry development is more. Molecular mass of a compound is important in determination of Character of a compound High resolution, accurate mass (precursor & products) tandem mass spectrometry technology needed • For quantitative selectivity (near isobaric crosstalk)- • For accurate qualitative identifications 1% FPR at peptide level (Decoy DB; Peptide Prophet) • No QCs = No Quantifiably Reliable Data Although several laboratories have generated useful quantitative proteomic data using state‐of‐the‐art mass spectrometry, no harmonized guidelines exit for sample analysis and data integration to in vivo translation practices

Quantitative mass spectrometry methods for pharmaceutical

  1. e their m/z. The basic components of a mass spectrometer are the ion source.
  2. Mass spectrometry in the quantitative analysis of therapeutic intracellular nucleotide analogs. Robert S. Jansen. Corresponding Author. robert.jansen@slz.nl; Department of Pharmacy & Pharmacology, Slotervaart Hospital/The Netherlands Cancer Institute, Louwesweg 6, 1066 EC Amsterdam, the Netherlands
  3. Quantitative Biological and Clinical Mass Spectrometry : An Introduction. Anthony I. Mallet Author: Anthony I. Mallet Date: 27 Apr 2018 Publisher: John Wiley and Sons Ltd ISBN10: 1119281237 Imprint: Wiley-Blackwell File size: 26 Mb Dimension: 150x 250x..
  4. We have combined classical subcellular fractionation with large-scale quantitative mass spectrometry to identify proteins that enrich specifically with peroxisomes of Saccharomyces cerevisiae.In two complementary experiments, isotope-coded affinity tags and tandem mass spectrometry were used to quantify the relative enrichment of proteins during the purification of peroxisomes

Quantitative Mass Spectrometry-based Proteomics IntechOpe

Quantitative Mass Spectrometry incorporates collaborative projects in which the Mass Spectrometry Group provides quantitative information about, typically, small molecules by GCMS, LCMS and LCMSMS or.. By applying quantitative mass spectrometry, this is an alternative way to identify biomarkers for early diagnosis and personalized medicine. We review the current quantitative mass spectrometric technologies and analyses that have been developed and applied in the last decade in the context of pancreatic cancer Quantitative mass spectrometry by Millard, Brian J., 1978, Heyden edition, in Englis In partic- ular, the application of quantitative mass spectrometry o ers new opportunity and great potential to develop innovative diagnostic and prognostic tests, to identify novel therapeutic targets, to allow the design of individualized patient treat- ment, and eventually to extend healthy life and reduce the burdens of illness and disability

Molecular Imaging - Imabiotec

Quantitative Mass Spectrometry Reveals Changes in Histone H2B Variants as Cells Undergo Inorganic Arsenic-Mediated Cellular Transformation* S Matthew Rea‡**, Tingting Jiang§**, Rebekah Eleazer‡, Meredith Eckstein‡, Alan G. Marshall§¶, and Yvonne N. Fondufe-Mittendorf‡ Exposure to inorganic arsenic, a ubiquitous environmen MAP-DIA: Model-based Analysis of Quantitative Proteomics from Data Independent Acquisition Mass Spectrometry Data independent acquisition (DIA) is a mode of mass spectrometry (MS) analysis that can generate MS/MS data for an unbiased selection of peptides, offering new opportunities to achieve more complete detection of peptides/proteins Mass spectrometry is all about creating ions from the composite neutral species present in the gas mixture/matrix and identifying the characteristic product ions of each compound on the basis of their mass-to-charge ratio, m/z, as is necessary for the MS for separation and detection of the compounds. Whatever strategy is adopted, EI o

Mass Analyzers (Mass Spectrometry) are used to determine the mass-to-charge ratio (m/z), this ratio is used to differentiate between molecular ions that were formed in the desolvating capillary. In order for a mass-to-charge ratio to be determined, the mass analyzer must be able to separate even the smallest masses Quantitative mass spectrometry identifies CDH2 interactome. (A) Plot of P-value (−log 10) versus fold-change (log 2) (described in Materials and Methods) of identified proteins. Dashed gray lines mark P=0.001 (y axis) and fold-change=10 (x axis). (B) Summary of numbers of identified peptides and proteins at each stage of further condition. The resulting mass spectrometry data has the advantage over other, qualitative, methods like laser scanning confocal fluorescence microscopy (LSCM) that it reflects the relative quantities of the compounds that have been identified. MALDI exploits a laser light-absorbing matrix to generate ions from large molecules with minimal fragmentation The detection system is a quadrupole mass spectrometer operating in the 1-340 amu range, supplemented with a secondary electron multiplier. The maximum analysable area is 14 mm in diameter

Mass spectrometry is a rapidly evolving measurement technique for synthetic polymers. It holds the promise of providing not only absolute molecular mass distributions but also quantitative end-group and repeat-unit composition, and structural information such as branching and intramolecular loop formation Chemical cross-linking mass spectrometry (XL-MS) provides protein structural information by identifying covalently linked proximal amino acid residues on protein surfaces. The information gained by this technique is complementary to other structural biology methods such as x-ray crystallography, NMR and cryo-electron microscopy[1]. The extension of traditional quantitative proteomics methods. Related papers. Page number / 15 1 Definition på engelska: Quantitative Mass Spectrometry Facility . Andra betydelser av QMSF Förutom Kvantitativa masspektrometri anläggning har QMSF andra betydelser. De listas till vänster nedan. Vänligen scrolla ner och klicka för att se var och en av dem. För alla betydelser av QMSF, vänligen klicka på mer

CLINSPECT-M: Clinical mass spectrometry center forGas Chromatography-Mass Spectrometry | Stratochem ServicesSPS MS3 Workflows | Thermo Fisher ScientificBITS - Introduction to Mass Spec data generationSeparations | Free Full-Text | Analyses of IndoleQ Exactive™ GC Orbitrap™ GC-MS/MS

Mass spectrometry for real-time quantitative breath analysis. David Smith 1,5, Patrik Španěl 2, Jens Herbig 3 and Jonathan Beauchamp 4. Published 28 March 2014 • 2014 IOP Publishing Ltd Journal of Breath Research, Volume 8, Number SILu ™ Prot Protein Standards for Quantitative Mass Spectrometry SILu ™ Prot products are a novel collection of stable isotope-labeled (SIL, or heavy labeled) full length proteins designed to be used as mass spectrometry internal standards for quantitative proteomics Mass spectrometry (MS) is one of the most powerful tools to study biomolecules including glycoproteins and glycans. With the continuous development of glycoproteomics and glycomics based on MS analysis, more and more techniques have appeared and contribute to understanding the structure and function of glycoproteins and glycans Mass spectrometry-based quantitative proteomics TATSUJI NAKAMURA AND YOSHIYA ODA* Laboratory of Seeds Finding Technology, Eisai Co., Ltd., Tokodai 5-1-3, Tsukuba, Ibaraki 300-2635, Japan Introduction The genomic era in the 1990s provided massive amounts of information about DN To use the mass spectrometry-based proteomics facility, contact Ganna by e-mail or telephone and book a time for a start-up meeting: Ganna Shevchenko 018-471 3686 ganna.shevchenko@kemi.uu.s MALDI-TOF MS is used for the qualitative analysis of seven different polymer additives directly from the polymer without tedious sample pretreatment. Additionally, by using a solid sample preparation technique, which avoids the concentration gradient problems known to occur with dried droplets and by adding tetraphenylporphyrine as an internal standard to the matrix, it is possible to perform.

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