Analyzing Biomolecular Interactions by Mass Spectrometry E-Book
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- Herausgeber: Wiley-VCH
- Kategorie: Wissenschaft und neue Technologien
- Sprache: Englisch
This monograph reviews all relevant technologies based on mass spectrometry that are used to study or screen biological interactions in general.
Arranged in three parts, the text begins by reviewing techniques nowadays almost considered classical, such as affinity chromatography and ultrafiltration, as well as the latest techniques. The second part focusses on all MS-based methods for the study of interactions of proteins with all classes of biomolecules. Besides pull down-based approaches, this section also emphasizes the use of ion mobility MS, capture-compound approaches, chemical proteomics and interactomics. The third and final part discusses other important technologies frequently employed in interaction studies, such as biosensors and microarrays.
For pharmaceutical, analytical, protein, environmental and biochemists, as well as those working in pharmaceutical and analytical laboratories.
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Seitenzahl: 792
Veröffentlichungsjahr: 2015
Ähnliche
Table of Contents
Cover
Related Titles
Title Page
Copyright
List of Contributors
Preface
Abbreviations
Chapter 1: Introduction to Mass Spectrometry, a Tutorial
1.1 Introduction
1.2 Figures of Merit
1.3 Analyte Ionization
1.4 Mass Analyzer Building Blocks
1.5 Tandem Mass Spectrometry
1.6 Data Interpretation and Analytical Strategies
1.7 Conclusion and Perspectives
References
Part I: Direct MS Based Affinity Techniques
Chapter 2: Studying Protein–Protein Interactions by Combining Native Mass Spectrometry and Chemical Cross-Linking
2.1 Introduction
2.2 Protein Analysis by Mass Spectrometry
2.3 Native MS
2.4 Chemical Cross-linking MS
2.5 Value of Combining Native MS with Chemical Cross-linking MS
2.6 Regulating the Giant
2.7 Capturing Transient Interactions
2.8 An Integrative Approach for Obtaining Low-Resolution Structures of Native Protein Complexes
2.9 Future Directions
References
Chapter 3: Native Mass Spectrometry Approaches Using Ion Mobility-Mass Spectrometry
3.1 Introduction
3.2 Sample Preparation
3.3 Electrospray Ionization
3.4 Mass Analyzers and Tandem MS Approaches
3.5 Ion Mobility
3.6 Data Processing
3.7 Challenges and Future Perspectives
References
Part II: LC-MS Based with Indirect Assays
Chapter 4: Methodologies for Effect-Directed Analysis: Environmental Applications, Food Analysis, and Drug Discovery
4.1 Introduction
4.2 Principle of Traditional Effect-Directed Analysis
4.3 Sample Preparation
4.4 Fractionation for Bioassay Testing
4.5 Miscellaneous Approaches
4.6 Bioassay Testing
4.7 Identification and Confirmation Process
4.8 Conclusion and Perspectives
References
Chapter 5: MS Binding Assays
5.1 Introduction
5.2 MS Binding Assays – Strategy
5.3 Application of MS Binding Assays
5.4 Summary and Perspectives
Acknowledgments
References
Chapter 6: Metabolic Profiling Approaches for the Identification of Bioactive Metabolites in Plants
6.1 Introduction to Plant Metabolic Profiling
6.2 Sample Collection and Processing
6.3 Hyphenated Techniques
6.4 Mass Spectrometry
6.5 Mass Spectrometric Imaging
6.6 Data Analysis
6.7 Future Perspectives
References
Chapter 7: Antivenomics: A Proteomics Tool for Studying the Immunoreactivity of Antivenoms
7.1 Introduction
7.2 Challenge of Fighting Human Envenoming by Snakebites
7.3 Toolbox for Studying the Immunological Profile of Antivenoms
7.4 First-Generation Antivenomics
7.5 Snake Venomics
7.6 Second-Generation Antivenomics
7.7 Concluding Remarks
Acknowledgments
References
Part III: Direct Pre- and On-Column Coupled Techniques
Chapter 8: Frontal and Zonal Affinity Chromatography Coupled to Mass Spectrometry
8.1 Introduction
8.2 Frontal Affinity Chromatography
8.3 Staircase Method
8.4 Simultaneous Frontal Analysis of a Complex Mixture
8.5 Multiprotein Stationary Phase
8.6 Zonal Chromatography
8.7 Nonlinear Chromatography
Acknowledgments
References
Chapter 9: Online Affinity Assessment and Immunoaffinity Sample Pretreatment in Capillary Electrophoresis–Mass Spectrometry
9.1 Introduction
9.2 Capillary Electrophoresis
9.3 Affinity Capillary Electrophoresis
9.4 Immunoaffinity Capillary Electrophoresis
9.5 Capillary Electrophoresis–Mass Spectrometry
9.6 Application of ACE–MS
9.7 Applications of IA-CE–MS
9.8 Conclusions
References
Chapter 10: Label-Free Biosensor Affinity Analysis Coupled to Mass Spectrometry
10.1 Introduction to MS-Coupled Biosensor Platforms
10.2 Strategies for Coupling Label-Free Analysis with Mass Spectrometry
10.3 New Sensor and MS Platforms, Opportunities for Integration
References
Part IV: Direct Post Column Coupled Affinity Techniques
Chapter 11: High-Resolution Screening: Post-Column Continuous-Flow Bioassays
11.1 Introduction
11.2 The High-Resolution Screening Platform
11.3 Data Analysis
11.4 Conclusions and Perspectives
References
Chapter 12: Conclusions
Index
End User License Agreement
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Guide
Cover
Table of Contents
Preface
Part I: Direct MS Based Affinity Techniques
Begin Reading
List of Illustrations
Figure 1.1
Figure 1.2
Figure 1.3
Figure 1.4
Figure 1.5
Figure 1.6
Figure 1.7
Figure 1.8
Figure 1.9
Figure 1.10
Figure 1.11
Figure 2.1
Figure 2.2
Figure 2.3
Figure 2.4
Figure 2.5
Figure 3.1
Figure 3.2
Figure 3.3
Figure 3.4
Figure 3.5
Figure 3.6
Figure 3.7
Figure 3.8
Figure 3.9
Figure 3.10
Figure 4.1
Figure 4.2
Figure 4.3
Figure 4.4
Figure 4.5
Figure 4.6
Figure 4.7
Figure 4.8
Figure 4.9
Figure 4.10
Figure 4.11
Figure 4.12
Figure 4.13
Figure 5.1
Figure 5.2
Figure 5.3
Figure 5.4
Figure 5.5
Figure 5.6
Figure 5.7
Figure 5.8
Figure 5.9
Figure 5.10
Figure 5.11
Figure 5.12
Figure 5.13
Figure 5.14
Figure 5.15
Figure 5.16
Figure 5.17
Figure 5.18
Figure 6.1
Figure 6.2
Figure 6.3
Figure 7.1
Figure 7.2
Figure 7.3
Figure 7.4
Figure 7.5
Figure 8.1
Figure 8.2
Figure 8.3
Figure 8.4
Figure 8.5
Figure 8.6
Figure 8.7
Figure 8.8
Figure 8.9
Figure 8.10
Figure 8.11
Figure 8.12
Figure 9.1
Figure 9.2
Figure 9.3
Figure 9.4
Figure 9.5
Figure 9.6
Figure 9.7
Figure 9.8
Figure 9.9
Figure 9.10
Figure 9.11
Figure 10.1
Figure 10.2
Figure 10.3
Figure 10.4
Figure 11.1
Figure 11.2
Figure 11.3
Figure 11.4
Figure 11.5
Figure 11.6
Figure 11.7
Figure 11.8
Figure 11.9
Figure 11.10
Figure 11.11
Figure 11.12
Figure 11.13
List of Tables
Table 1.1
Table 1.2
Table 1.3
Table 6.1
Table 8.1
Table 8.2
Table 8.3
Table 8.4
Table 9.1
Table 9.2
Table 9.3
Table 11.1
Table 11.2
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Edited byJeroen Kool and Wilfried M.A. Niessen
Analyzing Biomolecular Interactionsby Mass Spectrometry
The Editors
Dr. Jeroen Kool
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
Division of BioAnalytical Chemistry/ BioMolecular Analysis
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
Prof. Dr. Wilfried M.A. Niessen
hyphen MassSpec
de Wetstraat 8
2332 XT Leiden
The NetherlandsandVU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
Division of BioAnalytical Chemistry/\hb BioMolecular Analysis
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
All books published by Wiley-VCH are carefully produced. Nevertheless, authors, editors, and publisher do not warrant the information contained in these books, including this book, to be free of errors. Readers are advised to keep in mind that statements, data, illustrations, procedural details or other items may inadvertently be inaccurate.
Library of Congress Card No.: applied for
British Library Cataloguing-in-Publication Data
A catalogue record for this book is available from the British Library.
Bibliographic information published by the Deutsche Nationalbibliothek
The Deutsche Nationalbibliothek lists this publication in the Deutsche Nationalbibliografie; detailed bibliographic data are available on the Internet at <http://dnb.d-nb.de>.
© 2014 Wiley-VCH Verlag GmbH & Co. KGaA, Boschstr. 12, 69469 Weinheim, Germany
All rights reserved (including those of translation into other languages). No part of this book may be reproduced in any form – by photoprinting, microfilm, or any other means – nor transmitted or translated into a machine language without written permission from the publishers. Registered names, trademarks, etc. used in this book, even when not specifically marked as such, are not to be considered unprotected by law.
Print ISBN: 978-3-527-33464-3
ePDF ISBN: 978-3-527-67342-1
ePub ISBN: 978-3-527-67341-4
Mobi ISBN: 978-3-527-67340-7
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List of Contributors
David Bonnel
ImaBiotech
Parc Eurasanté
885 av. Eugène Avinée
59120 Loos
France
Angela I. Calderón
Auburn University
Harrison School of Pharmacy
Department of Drug Discovery and Development
4306 Walker Building
Auburn
AL 36849
USA
Juan J. Calvete
Institut de Biomedicina de València-CSIC
C/Jaume Roig, 11
46010 València
Spain
David Falck
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
and
Leiden University Medical Center (LUMC)
Center for Proteomics and Metabolomics
Division of Glycomics and Glycoproteomics
Albinusdreef 2
2300RC Leiden
The Netherlands
José María Gutiérrez
Universidad de Costa Rica
Instituto Clodomiro Picado
Facultad de Microbiología
San José
Costa Rica
Rob Haselberg
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
Georg Höfner
Ludwig-Maximilians-Universität
Department für Pharmazie
Butenandtstr. 7
81377 München
Germany
Corine Houtman
VU University Amsterdam
Faculty of Earth and Life Sciences
Institute for Environmental Studies
De Boelelaan 1087
1081 HV Amsterdam
The Netherlands
Zhenjing Jiang
Jinan University
Department of Pharmacy and Guangdong Province Key Laboratory of Pharmacodynamic Constituents of Traditional Chinese Medicine and New Drug Research
Guangzhou 510632
China
Willem Jonker
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
Division of BioAnalytical Chemistry/BioMolecular Analysis
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
Albert Konijnenberg
University of Antwerpen
Department of Chemistry
Biomolecular and Analytical Mass Spectrometry
Groenenborgerlaan 171
2020 Antwerpen
Belgium
Jeroen Kool
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
Marja Lamoree
VU University Amsterdam
Faculty of Earth and Life Sciences
Institute for Environmental Studies
De Boelelaan 1087
1081 HV Amsterdam
The Netherlands
Filip Lemière
University of Antwerpen
Department of Chemistry
Biomolecular and Analytical Mass Spectrometry
Groenenborgerlaan 171
2020 Antwerpen
Belgium
Frederik Lermyte
University of Antwerpen
Department of Chemistry
Biomolecular and Analytical Mass Spectrometry
Groenenborgerlaan 171
2020 Antwerpen
Belgium
Bruno Lomonte
Universidad de Costa Rica
Instituto Clodomiro Picado
Facultad de Microbiología
San José
Costa Rica
Gerardo R. Marchesini
Plasmore S.r.l.
Via G. Deledda 4
21020 Ranco (Varese)
Italy
Esther Marie Martin
University of Antwerpen
Department of Chemistry
Biomolecular and Analytical Mass Spectrometry
Groenenborgerlaan 171
2020 Antwerpen
Belgium
Dora Mehn
Fondazione Don Carlo Gnocchi Onlus, Via Capecelatro 66
20148 Milano
Italy
Ruin Moaddel
National Institute on Aging
National Institutes of Health
Bioanalytical Chemistry and Drug Discovery Section
Biomedical Research Center
251 Bayview Boulevard
Suite 100
Baltimore, MD 21224-6825
USA
and
Jinan University
Department of Pharmacy and Guangdong Province Key Laboratory of Pharmacodynamic Constituents of Traditional Chinese Medicine and New Drug Research
Guangzhou 510632
China
Wilfried M.A. Niessen
hyphen MassSpec
de Wetstraat 8
2332 XT Leiden
The Netherlands
and
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
Emily Pipan
Auburn University
Harrison School of Pharmacy
Department of Drug Discovery and Development
4306 Walker Building
Auburn, AL 36849
USA
Davinia Pla
Institut de Biomedicina de València-CSIC
C/Jaume Roig, 11
46010 València
Spain
Libia Sanz
Institut de Biomedicina de València-CSIC
C/Jaume Roig, 11
46010 València
Spain
Michal Sharon
Weizmann Institute of Science
Department of Biological Chemistry
234 Herzl Street
Rehovot 76100
Israel
Nagendra S. Singh
National Institute on Aging
National Institutes of Health
Bioanalytical Chemistry and Drug Discovery Section
Biomedical Research Center
251 Bayview Boulevard
Suite 100
Baltimore, MD 21224-6825
USA
Andrea Sinz
Martin-Luther University Halle-Wittenberg
Institute of Pharmacy
Wolfgang-Langenbeck-Straße 4
06120 Halle (Saale)
Germany
Frank Sobott
University of Antwerpen
Department of Chemistry
Biomolecular and Analytical Mass Spectrometry
Groenenborgerlaan 171
2020 Antwerpen
Belgium
Govert W. Somsen
VU University Amsterdam
Faculty of Science
Amsterdam Institute for Molecules Medicines and Systems
Division of BioAnalytical Chemistry/BioMolecular Analysis
De Boelelaan 1083
1081 HV Amsterdam
The Netherlands
Klaus T. Wanner
Ludwig-Maximilians-Universität
Department für Pharmazie – Zentrum für Pharmaforschung
Butenandtstraße 7
81377 München
Germany
Preface
The introduction, in 1988, of two new ionization methods for mass spectrometry (MS) has greatly changed the application areas of MS, especially in the biochemical and biological fields. Electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI) enabled the efficient analysis of highly polar biomolecules as well as complex biomacromolecules in an easy and user-friendly way and with excellent sensitivity. Multiple charging of proteins in ESI-MS enables the use of simple and relatively cheap mass analyzers in the analysis of peptides and proteins and even opened the way to study intact noncovalent complexes of proteins and drugs or other molecules, including protein–protein complexes. In addition, ESI provided an excellent means to perform online coupling of liquid chromatography (LC) to MS. MALDI-MS with its high level of user-friendliness and excellent sensitivity also boosted the applications of MS in studying biomacromolecules, being more recently even extended to the characterization of complete microorganisms. These developments encouraged further instrumental developments toward highly advanced (and more expensive) mass spectrometers, which provide additional possibilities in the study of biomolecules and their interactions. These new technologies opened a wide range of new application areas, of which perhaps proteomics and all derived strategies and applications belong to the most marked accomplishments. ESI-MS and MALDI-MS changed the way biochemists and biologists perform their research into molecular structures and (patho)physiological processes. Along similar lines, it also changed the ways drug discovery and development is being performed within the pharmaceutical industries. And in the slipstream of this, it changed analytical chemical research efforts in many other application areas.
The ability to study intact biomacromolecules and especially noncovalent complexes between biomolecules as well as other developments in the field, initiated by the introduction of ESI-MS and MALDI-MS, opened extensive research into the way MS can be used in the study of biomolecular interactions. Different distinct areas for analysis of bioaffinity interactions, and for analysis of biologically active molecules in general, can be recognized in this regard. These areas include precolumn-based ligand trapping followed by MS analysis, affinity chromatography following MS, and postcolumn online affinity profiling. Other methodologies are more indirect and relate to separately performed bioassays and (LC)-MS analysis, such as effect-directed analysis, metabolic profiling, and antivenomics approaches. Besides these, direct approaches without the use of chromatography are nowadays also used in several research areas. These include direct MS-based bioassays and native MS studies in which the latter looks at intact protein complexes in the gas phase. Affinity techniques for trapping proteins and protein complexes toward bottom-up proteomics analysis could also be mentioned in this regard although these techniques are actually specific sample preparation strategies for proteomics research.
With so many new approaches and technologies being introduced in this area in the past 10–15 years, it seems appropriate to compile a thorough review of the current state of the art in the analysis of biomolecular interactions by MS. That is what this book provides in 12 chapters. Apart from a tutorial chapter on MS in the beginning and a conclusive overview at the end of the book, the various chapters are grouped into four themes:
Native MS, that is, the study of liquid-phase and gas-phase protein–protein interactions by MS and ion-mobility MS
The use of LC–MS to study biomolecular interactions via indirect assays, as, for instance, applied in effect-directed analysis and related approaches, MS-based binding and activity assays, and other ways to study and identify bioactive molecules, for example, via metabolic profiling or antivenomics.
Precolumn and on-column technologies to assess bioaffinity, involving frontal and zone affinity chromatography, ultrafiltration and size exclusion chromatography, affinity capillary electrophoresis, and biosensor affinity analysis coupled to MS.
Online postcolumn continuous-flow bioassays to study bioactivity or bioaffinity of compounds after chromatographic separation.
The contributors to this book did a great job in writing very good reviews and providing beautiful artwork to illustrate the principles and applications of their specific areas within the analysis of biomolecular interactions by MS. For us, it was a pleasure to work with them in this project. We would like to thank them all for their work and for their patience with us in finalizing the final versions of the various chapters.
We hope the readers will benefit from this book, value the overview provided in the various chapters, and perhaps even get stimuli for new research areas or new approaches to perform their research, for instance, by combining ideas and approaches from various chapters of the book into new advanced technologies.
Enjoy reading and get a high affinity with MS!
August 2014
Jeroen Kool and Wilfried NiessenVU University Amsterdam, Faculty of Science,Amsterdam Institute for Molecules,Medicines and Systems, Division of BioAnalytical,Chemistry/BioMolecular AnalysisAmsterdam,Netherlands
Abbreviations
μ
Electrophoretic mobility
2DE
Two-dimensional electrophoresis
5-HT
5-Hydroxytryptamine, serotonin
5-HT
2A
5-Hydroxytryptamine (serotonin) receptor subtype 2A
Ab
Antibody
ACE
Affinity capillary electrophoresis
ACE
Angiotensin converting enzyme
AChBP
Acetyl choline binding protein
Ag
Antigen
Ag–Ab
Antigen–antibody complex
AhR
Aryl hydrocarbon receptor
AMAC
Accelerated membrane assisted clean-up
APCI
Atmospheric pressure chemical ionization
API
Atmospheric pressure ionization
AR-CALUX
Androgen chemically activated luciferase expression
BGE
Background electrolyte
BGF
Bioassay guided fractionation
BGT1
Betaine-GABA transporter
BLAST
Basic local alignment search tool
BS
2
G
Bis(sulfosuccinimidyl)suberate
CCT
Chaperonin containing Tcp1
CDER
Center for drug evaluation and research
CE
Capillary electrophoresis
CECs
Chemicals of emerging concern
CHCA
α-Cyano-4-hydroxy cinnamic acid
CI
Chemical ionization
CID
Collision-induced dissociation
CID-MS/MS
Collision-induced dissociation tandem mass spectrometry
CRISPR
Clustered regularly interspaced short palindromic repeat
CZE
Capillary zone electrophoresis
D
1–5
Dopamine receptor subtypes D1 to D5
DAD
Diode array detector
DCC
Dynamic combinatorial chemistry
DCL
Dynamic combinatorial library
DDA
Data dependent acquisition
DVB/CAR/PDMS
Divinyl-benzene/carboxen/polydimethylsiloxane
EC
Electrochemical conversion
ECD
Electron-capture dissociation
EDA
Effect-directed analysis
EI
Electron ionization
EIC
Extracted ion chromatograms
EICs
Extracted ion currents
ELSD
Evaporative light scattering detection
EOF
Electroosmotic flow
ER
Estrogen receptor
EROD
Ethoxyresorufin-
O
-deethylase
ESI
Electron spray ionization
ESI
Electrospray ionization
ESI-MS
Electrospray-ionization mass spectrometry
ETD
Electron-transfer dissociation
FA
Formic acid
FA
Frontal analysis
Fab
Fragment antigen-binding
FACCE
Frontal analysis continuous capillary electrophoresis
FDA
US Food and Drug Administration
FIA
Flow-injection analysis
FLD
Fluorescence detection
FRAP
Ferric reducing antioxidant power
FRET
Fluorescence resonance energy transfer
FWHM
Full width at half maximum
GABA
γ-Aminobutyric acid
GAT1–3
GABA transporter subtypes 1–3 (according to HUGO)
GC–MS
Gas chromatography mass spectrometry
GC-O
Gas chromatography olfactometry
GCxGC
Comprehensive two dimensional gas chromatography
GPC
Gel permeation chromatography
GPCR
G protein-coupled receptor
GSI
Global snakebite initiative
GST
Glutathione-
S
-transferase
HBH
Histidine–biotin–histidine
HDX
Hydrogen–deuterium exchange
HEK
Human embryonic kidney cells
HPLC
High performance liquid chromatography
HRS
High-resolution screening
HTLC
High-temperature liquid chromatography
HTS
High throughput screening
I.D.
Inner diameter
IA-CE
Immunoaffinity capillary electrophoresis
IC
50
Half maximal inhibitory concentration
ICP
Inductively coupled plasma
ICP-MS
Inductively coupled plasma MS
ID
Inner diameter
IMS
Ion mobility spectrometry
ISD
In-source decay
IT
Ion-trap MS
IT-TOF
Tandem ion-trap – time-of-flight MS
K
a
Association constant
K
d
Dissociation constant
K
d
Equilibrium dissociation constant
kDa
kilodalton (10
3
Da)
K
i
Affinity constant
k
off
Rate constant of complex dissociation
k
on
Rate constant of complex formation
L
Ligand
LC
Liquid chromatography
LC–MS
Liquid chromatography mass spectrometry
LC–MS
E
Liquid chromatography mass spectrometry in an alternating energy mode
LIF
Laser induced fluorescence
LLE
Liquid liquid extraction
LLOQ
Lower limit of quantification
MALDI
Matrix assisted laser desorption ionization
MS
Mass spectrometry/mass spectrometer
MS/MS
Tandem mass spectrometry
MTS
3-(4,5-Dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium
MTT
3-(4,5-Dimethyldiazol-2-yl)-2,5 diphenyl tetrazolium bromid
nAChR
Nicotinic acetylcholine receptor
NECEEM
Non-equilibrium capillary electrophoresis of equilibrium mixtures
NHS
N
-Hydroxysuccinimide
NMR
Nuclear magnetic resonance
NMR
Nuclear magnetic resonance spectrometry
np-HPLC
Normal phase high performance liquid chromatography
p38
p38 mitogen-activated protein kinase
PAHs
Poly aromatic hydrocarbons
PDE
Phosphodiesterase
PEEK
Polyether ether ketone
PEG
Polyethylene glycol
PLE
Pressurized liquid extraction
POCIS
Polar organic chemical integrative sampler
PTFE
Polytetrafluoroethylene
QSAR
Quantitative structure–activity relationships
QTAX
Quantitative analysis of tandem affinity purified
in vivo
cross-linked protein complexes
Q-TOF
Quadrupole time-of-flight
q-TOF
Tandem quadropule – time-of-flight MS
R
Receptor
rhSHBG
Recombinant human sex hormone binding globulin
RL
Receptor–ligand complex
RP
Reverse-phase
RP-HPLC
Reverse-phase high-performance liquid chromatography
RP-LC
Reversed phase LC
rTTR
Recombinant transthyretin
SAFE
Solvent assisted flavor extraction
SAXS
Small-angle X-ray scattering
SBSE
Stir bar sorptive extraction
SD
Standard deviation
SDS-PAGE
Sodium dodecyl sulfate polyacrylamide gel electrophoresis
SEC
Size exclusion chromatography
sEH
Soluble epoxide hydrolase
SERT
Serotonin transporter
SID
Surface-induced dissociation
SILAC
Stable isotope labeling of amino acids in cell culture
SLC6
Solute carrier family 6
SPE
Solid phase extraction
SPMD
Semi permeable membrane device
SPME
Solid phase microrxtraction
SRM
Selected reaction monitoring mode
T
4
Thyroxin
T
4
*
Radiolabeled thyroxin
TAP
Tandem affinity purification
TCA
Tricyclic antidepressants
TFA
Trifluoroacetic acid
TIC
Total ion chromatograms
TIE
Toxicity identity evaluation
TLC
Thin layer chromatography
TOF
Time-of-flight
TP
Transformation product
TTR
Transthyretin
UPLC
Ultra performance liquid chromatography
UV
Ultraviolet
UV/vis
Ultra violet/visible spectroscopy
WHO
World Health Organization
YAS
Yeast androgen screen
YES
Yeast estrogen screen
1Introduction to Mass Spectrometry, a Tutorial
Wilfried M.A. Niessen and David Falck
1.1 Introduction
In the past 30 years, mass spectrometry (MS) has undergone a spectacular development, in terms of both its technological innovation and its extent of application. On-line liquid chromatography–mass spectrometry (LC–MS) has become a routine analytical tool, important in many application areas. The introduction of electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) has enabled the MS analysis of highly polar and large molecules, including biomacromolecules. MS is based on the generation of gas-phase analyte ions, the separation of these ions according to their mass-to-charge ratio (/), and the detection of these ions. A wide variety of ionization techniques are available to generate analyte ions (Section 1.3). Mass analysis can be performed by six types of mass analyzers (Section 1.4), although quite frequently tandem mass spectrometers, featuring the combination of two mass analyzers, are used (Section 1.5). The data acquired by MS allow quantitative analysis of target analytes, determination of the molecular mass/weight, and/or structure elucidation or sequence determination of (unknown) analytes (Section 1.6).
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
Lesen Sie weiter in der vollständigen Ausgabe!
