MALDI MS: a practical guide to instrumentation, methods and applications
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| Format: | Buch |
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| Sprache: | English |
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WILEY-VCH
2007
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| Online-Zugang: | Inhaltstext Inhaltsverzeichnis |
| Beschreibung: | XVI, 345 S. Ill., graph. Darst. 240 mm x 170 mm |
| ISBN: | 9783527314409 3527314407 |
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| 245 | 1 | 0 | |a MALDI MS |b a practical guide to instrumentation, methods and applications |c ed. by Franz Hillenkamp ... |
| 264 | 1 | |a Weinheim |b WILEY-VCH |c 2007 | |
| 300 | |a XVI, 345 S. |b Ill., graph. Darst. |c 240 mm x 170 mm | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 4 | |a Espectrometría de masas | |
| 650 | 4 | |a Matrix-assisted laser desorption-ionization | |
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Datensatz im Suchindex
| _version_ | 1805088412492890112 |
|---|---|
| adam_text |
V
Contents
Preface XI
List of Contributors XV
1 The MALDI Process and Method 1
Franz Hillenkamp and Michael Karas
1.1 Introduction 1
1.2 Analyte Incorporation 3
1.3 Absorption of the Laser Radiation 5
1.4 The Ablation/Desorption Process 7
1.5 Ionization 11
1.6 Fragmentation of MALDI Ions 14
1.7 MALDI of Non Covalent Complexes 16
1.8 The Correct Choice of Matrix: Sample Preparation 18
1.8.1 Surface Preparation 20
1.8.2 Anchor Sample Plates 21
References 23
2 MALDI Mass Spectrometry Instrumentation 29
Peter B. O'Connor and Franz Hillenkamp
2.1 Introduction 29
2.2 Lasers for MALDI MS 30
2.3 Fragmentation of MALDI Ions 35
2.3.1 MALDI at Elevated Pressure 36
2.3.2 Tandem Mass Spectrometry of MALDI Ions 37
2.4 Mass Analyzers 39
2.4.1 Axial TOF Mass Spectrometers 41
2.4.2 Reflectron TOF Mass Spectrometers 43
2.4.3 Tandem TOF Mass Spectrometers 44
2.4.4 Orthogonal TOF Mass Analyzers 48
2.4.5 Tandem Mass Spectrometry in oTOF Mass Analyzers 49
2.4.6 Ion Detectors and Data Processing in MALDI TOF analyzers 49
2.5 Fourier Transform Ion Cyclotron Resonance Mass Spectrometers 52
MA! Dl MS A Rractuiil Guidt to Instrumentation. Mt thods and Applications.
Fdited bv Franz Hillenkamp and Jasna Peter Katalimc
Copyright © 2(X)7 Wiley VCH Verlag GmbH Co. KGaA. Weinheim
ISBN: 978 3 527 31440 9
VI Contents
2.5.1 Tandem Mass Spectrometry on FTICR mass Spectrometers 58
2.6 Quadrupole Ion Trap Mass Spectrometers 60
2.6.1 RF Only Ion Guides and LIT Mass Spectrometers 64
2.6.2 Tandem Mass Spectrometry on QIT Mass Spectrometers 65
2.7 Hybrid Mass Spectrometers 66
2.7.1 Quadrupole TOF Mass Spectrometers 66
2.7.2 Quadrupole FT Mass Spectrometers 68
2.7.3 QIT TOF Mass Spectrometers 69
2.7.4 Orbitrap 71
2.8 Future Directions 72
References 75
3 MALDI MS in Protein Chemistry and Proteomics 83
Karin Hjemo and Ole N. Jensen
3.1 Introduction 83
3.2 Sample Preparation for Protein and Peptide Analysis by
MALDI MS 86
3.3 Strategies for Using MALDI MS in Protein Biochemistry 89
3.3.1 Peptide Mass Mapping of Purified Proteins 91
3.3.2 Peptide Sequencing by MALDI MS/MS 92
3.3.3 Analysis of Post Translational Modifications 94
3.4 Applications of MALDI MS in Proteomics 97
3.4.1 Protein Identification by MALDI MS Peptide Mass Mapping 97
3.4.2 Quantitation of Proteins by MALDI MS 100
3.5 Computational Tools for Protein Analysis by MALDI MS 101
3.6 Clinical Applications of MALDI MS 102
3.7 Conclusions 103
References 104
4 Microprobing and Imaging MALDI for Biomarker Detection 109
Bernhard Spengler
4.1 Introduction 109
4.2 History of Mass Spectrometry Imaging and Microprobing
Techniques 112
4.3 Visualization of Mass Spectrometric Information 113
4.4 MALDI in Micro Dimensions: Instruments and Mechanistic
Differences 116
4.5 The Matrix Deposition Problem in High Resolution Imaging 118
4.6 Organisms, Organs, Tissues and Cells: Imaging MALDI at Various
Lateral Resolutions 120
4.7 Whole Cell and Single Cell Analysis: Prospects and Limitations 122
4.7.1 Cellular Analysis 123
4.7.2 Individually Isolated Cells 124
4.7.3 Direct Cellular and Subcellular Imaging 124
4.8 Cell Sorting and Capturing 124
4.9 Future Areas of Application 125
Contents I VII
4.10 Identification and Characterization: Limitations Due to Mass Resolution
and Accuracy 126
4.11 Conclusions 127
References 127
5 MALDI MS of Nucleic Acids and Practical Implementations in Cenomics
and Genetics 131
Dirk van den Boom and Stefan Berkenkamp
5.1 Challenges in Nucleic Acid Analysis by MALDI MS 131
5.2 Genetic Markers 136
5.2.1 Restriction Fragment Length Polymorphisms (RFLPs) 137
5.2.2 Microsatellites/Short Tandem Repeats (STRs) 138
5.2.3 Single Nucleotide Polymorphisms (SNPs) 139
5.2.3.1 The HapMap 140
5.3 Assay Formats for Nucleic Acid Analysis by MALDI MS 240
5.4 Applications in Genotyping 142
5.4.1 MALDI TOF MS SNP and Mutation Analysis 142
5.4.1.1 The PinPoint Assay 143
5.4.1.2 The PROBE Assay 145
5.4.1.3 The MassEXTEND, hME Assay 146
5.4.1.4 The GOOD Assay 148
5.4.1.5 The Invader Assay ISO
5.4.1.6 Incorporation and Complete Chemical Cleavage Assay 150
5.4.1.7 The Restriction Fragment Mass Polymorphism Assay 152
5.4.2 MALDI TOF MS for Haplotyping 153
5.5 Applications of Comparative Sequence Analysis 155
5.5.1 Base Specific Cleavage of Amplification Products 258
5.5.1.1 DNA Based Methods 159
5.5.1.2 RNA Based Methods 260
5.5.1.3 Analysis of Base Specific Cleavage Patterns 161
5.6 Applications in Quantitation of Nucleic Acids for Analysis of Gene
Expression and Gene Amplification 265
5.6.1 Analysis of DNA Mixtures and Allele Frequency Determinations in DNA
Pools 265
5.6.2 Analysis of Gene Expression 369
References 172
6 MALDI MS of Clycans 282
Dijana S*agi andjasna Peter Katalinic
6.1 Introduction 282
6.2 N Glycosylation 282
6.2.1 Release of N Glycans 284
6.2.1.1 Chemical Release 284
6.2.1.2 Enzymatic Release 284
6.2.2 Sample Preparation for MALDI MS 287
VIII I Contents
6.2.2.1 Contaminant Removal 187
6.2.2.2 Derivatization 187
6.2.3 Matrices 189
6.2.3.1 Matrices for Neutral N Glycans 189
6.2.3.2 Matrices for Acidic N Glycans 191
6.2.4 Structural Analysis 191
6.2.4.1 Fragmentation of N Glycans 191
6.2.4.2 Post Source Decay 194
6.2.4.3 Collision Induced Decomposition 195
6.2.4.4 Use of Exoglycosidase Sequencing 199
6.2.5 MALDI MS of Intact Glycoproteins 199
6.2.6 Determination of N Glycosylation Site Occupancy 201
6.3 O Glycosylation 203
6.3.1 Release of O Glycans from the Parent Protein 204
6.3.2 MALDI TOF MS of Released O Glycans 205
6.3.3 Determination of O Glycosylation Sites by PSD MALDI TOF MS 205
6.3.4 Determination of O Glycosylation Status by MALDI TOF MS 206
6.3.5 Identification of O Glycosylation in Proteins by In Gel
Alkylaminylation 206
6.3.6 O Glycoforms in Urine: Identification of O Glycosylated Amino Acids in
Mixtures by MALDI MS and Computer Assignment 207
6.3.7 Identification of the Non Covalent O Glycoprotein Dimer by Blot
IR MALDI MS 209
6.3.8 Determination of Overall O Glycosylation of a Glycoprotein by
Permethylation 209
References 210
7 MALDI MS of Lipids 215
Jurgen Schiller
7.1 Introduction 215
7.1.1 Why are Lipids of Interest? 215
7.1.2 Problems in Lipid Analysis: A Brief Comparison of Methods 217
7.1.3 Analysis of Lipids by MS 217
7.1.4 Capabilities and Limitations of MALDI TOF MS in the
Lipid Analysis 218
7.1.5 Choosing an Appropriate Matrix 219
7.1.6 Sample Preparation, Extraction and Purification 221
7.2 Analysis of Individual Lipid Classes and their Characteristics 222
7.2.1 The Apolar Lipids: Diacylglycerols, Triacylglycerols, Cholesterol and
Cholesteryl Esters 222
7.2.2 Zwitterionic Phospholipids: Sphingomyelin, Phosphatidylcholine and
Phosphatidylethanolamine 224
7.2.3 Acidic Phospholipids: Phosphatidic Acid, Cardiolipin,
Phosphatidylglycerol, Phosphatidylserine, Inositol and Higher
Phosphoinositides and their Lysolipids 227
Contents IIX
7.2.4 Free Fatty Acids 228
7.3 MALDI TOF MS of Typical Lipid Mixtures 229
7.3.1 Vegetable Oils and Frying Fats 229
7.3.2 Plant and Tissue Extracts 229
7.3.2.1 Brain Phospholipids 230
7.3.2.2 Eye Lens Phospholipids 231
7.3.2.3 Other tissues 231
7.3.3 Important Body Fluids and Cells of the Human Body 231
7.3.3.1 Blood 232
7.3.3.2 Spermatozoa and Neutrophils 232
7.3.4 Characterization of Typical Oxidation Products of Lipids 235
7.4 Quantitative Aspects of MALDI TOF MS of Lipids 236
7A.I Approaches Used To Date 236
7.5 Problems, and their Potential Solution 237
7.5.1 "Small" Molecules and Fragmentation Products 237
7.5.2 Auxiliary Reagents 238
7.6 Summary and Outlook 238
References 240
8 MALDI MS for Polymer Characterization 245
Liang Li
8.1 Introduction 245
8.2 Technical Aspects of MALDI MS 246
8.2.1 Sample Preparation Issues 246
8.2.1.1 Matrix 247
8.2.1.2 Cationization Reagent 249
8.2.1.3 Solvent 251
8.2.1.4 Solvent Free Sample Preparation 257
8.2.2 Instrumental and Measurement Issues 258
8.2.2.1 Mass Resolution and Accuracy 258
8.2.2.2 Sensitivity and Dynamic Range 263
8.2.2.3 Mass Range 267
8.2.2.4 MS/MS Capability 270
8.2.3 Data Processing Issues 273
8.3 Attributes and Limitations of MALDI MS 276
8.4 Conclusions and Perspectives 285
References 286
9 Small Molecule Desorption/lonization Mass Analysis 299
Lucinda Cohen, Eden P. Co, and Gary Siuzdak
9.1 Introduction 299
9.2 Matrix Choices for Small Molecule MALDI 300
9.2.1 Organic Matrices 300
9.2.2 Inorganic Matrices 301
9.2.3 Liquid Matrices 303
X Contents
9.2.4 Matrix Free Approaches 304
9.3 Sample Preparation 307
9.3.1 Electrospray Sample Deposition 308
9.3.2 Analyte Derivatization 308
9.3.3 Analyte Pre Concentration 309
9.3.3.1 Prestructured Sample Supports 309
9.3.3.2 DIOS with Solid Liquid Extraction 310
9.3.4 Matrix Suppression 312
9.4 Qualitative Characterization of LMM Molecules 315
9.5 Analyte Quantitation by MALDI 318
9.5.1 Selection of IS 318
9.5.2 Methods for Improving Quantitative Performance 319
9.5.3 Quantitation of Pharmaceutical Compounds 320
9.5.4 Enzyme Activity and Inhibition Studies 322
9.5.5 Quantitative Analysis of Samples from Complex Biological
Matrices 323
9.5.6 Environmental Applications of Quantitative MALDI 324
9.6 Separation Methods Coupled with MALDI and DIOS 326
9.6.1 TLC MALDI 326
9.6.2 Capillary and Frontal Affinity Liquid Chromatography 328
9.7 Conclusions 331
References 333
Index 339 |
| adam_txt |
V
Contents
Preface XI
List of Contributors XV
1 The MALDI Process and Method 1
Franz Hillenkamp and Michael Karas
1.1 Introduction 1
1.2 Analyte Incorporation 3
1.3 Absorption of the Laser Radiation 5
1.4 The Ablation/Desorption Process 7
1.5 Ionization 11
1.6 Fragmentation of MALDI Ions 14
1.7 MALDI of Non Covalent Complexes 16
1.8 The Correct Choice of Matrix: Sample Preparation 18
1.8.1 Surface Preparation 20
1.8.2 Anchor Sample Plates 21
References 23
2 MALDI Mass Spectrometry Instrumentation 29
Peter B. O'Connor and Franz Hillenkamp
2.1 Introduction 29
2.2 Lasers for MALDI MS 30
2.3 Fragmentation of MALDI Ions 35
2.3.1 MALDI at Elevated Pressure 36
2.3.2 Tandem Mass Spectrometry of MALDI Ions 37
2.4 Mass Analyzers 39
2.4.1 Axial TOF Mass Spectrometers 41
2.4.2 Reflectron TOF Mass Spectrometers 43
2.4.3 Tandem TOF Mass Spectrometers 44
2.4.4 Orthogonal TOF Mass Analyzers 48
2.4.5 Tandem Mass Spectrometry in oTOF Mass Analyzers 49
2.4.6 Ion Detectors and Data Processing in MALDI TOF analyzers 49
2.5 Fourier Transform Ion Cyclotron Resonance Mass Spectrometers 52
MA! Dl MS A Rractuiil Guidt to Instrumentation. Mt thods and Applications.
Fdited bv Franz Hillenkamp and Jasna Peter Katalimc
Copyright © 2(X)7 Wiley VCH Verlag GmbH Co. KGaA. Weinheim
ISBN: 978 3 527 31440 9
VI Contents
2.5.1 Tandem Mass Spectrometry on FTICR mass Spectrometers 58
2.6 Quadrupole Ion Trap Mass Spectrometers 60
2.6.1 RF Only Ion Guides and LIT Mass Spectrometers 64
2.6.2 Tandem Mass Spectrometry on QIT Mass Spectrometers 65
2.7 Hybrid Mass Spectrometers 66
2.7.1 Quadrupole TOF Mass Spectrometers 66
2.7.2 Quadrupole FT Mass Spectrometers 68
2.7.3 QIT TOF Mass Spectrometers 69
2.7.4 Orbitrap 71
2.8 Future Directions 72
References 75
3 MALDI MS in Protein Chemistry and Proteomics 83
Karin Hjemo and Ole N. Jensen
3.1 Introduction 83
3.2 Sample Preparation for Protein and Peptide Analysis by
MALDI MS 86
3.3 Strategies for Using MALDI MS in Protein Biochemistry 89
3.3.1 Peptide Mass Mapping of Purified Proteins 91
3.3.2 Peptide Sequencing by MALDI MS/MS 92
3.3.3 Analysis of Post Translational Modifications 94
3.4 Applications of MALDI MS in Proteomics 97
3.4.1 Protein Identification by MALDI MS Peptide Mass Mapping 97
3.4.2 Quantitation of Proteins by MALDI MS 100
3.5 Computational Tools for Protein Analysis by MALDI MS 101
3.6 Clinical Applications of MALDI MS 102
3.7 Conclusions 103
References 104
4 Microprobing and Imaging MALDI for Biomarker Detection 109
Bernhard Spengler
4.1 Introduction 109
4.2 History of Mass Spectrometry Imaging and Microprobing
Techniques 112
4.3 Visualization of Mass Spectrometric Information 113
4.4 MALDI in Micro Dimensions: Instruments and Mechanistic
Differences 116
4.5 The Matrix Deposition Problem in High Resolution Imaging 118
4.6 Organisms, Organs, Tissues and Cells: Imaging MALDI at Various
Lateral Resolutions 120
4.7 Whole Cell and Single Cell Analysis: Prospects and Limitations 122
4.7.1 Cellular Analysis 123
4.7.2 Individually Isolated Cells 124
4.7.3 Direct Cellular and Subcellular Imaging 124
4.8 Cell Sorting and Capturing 124
4.9 Future Areas of Application 125
Contents I VII
4.10 Identification and Characterization: Limitations Due to Mass Resolution
and Accuracy 126
4.11 Conclusions 127
References 127
5 MALDI MS of Nucleic Acids and Practical Implementations in Cenomics
and Genetics 131
Dirk van den Boom and Stefan Berkenkamp
5.1 Challenges in Nucleic Acid Analysis by MALDI MS 131
5.2 Genetic Markers 136
5.2.1 Restriction Fragment Length Polymorphisms (RFLPs) 137
5.2.2 Microsatellites/Short Tandem Repeats (STRs) 138
5.2.3 Single Nucleotide Polymorphisms (SNPs) 139
5.2.3.1 The HapMap 140
5.3 Assay Formats for Nucleic Acid Analysis by MALDI MS 240
5.4 Applications in Genotyping 142
5.4.1 MALDI TOF MS SNP and Mutation Analysis 142
5.4.1.1 The PinPoint Assay 143
5.4.1.2 The PROBE Assay 145
5.4.1.3 The MassEXTEND, hME Assay 146
5.4.1.4 The GOOD Assay 148
5.4.1.5 The Invader Assay ISO
5.4.1.6 Incorporation and Complete Chemical Cleavage Assay 150
5.4.1.7 The Restriction Fragment Mass Polymorphism Assay 152
5.4.2 MALDI TOF MS for Haplotyping 153
5.5 Applications of Comparative Sequence Analysis 155
5.5.1 Base Specific Cleavage of Amplification Products 258
5.5.1.1 DNA Based Methods 159
5.5.1.2 RNA Based Methods 260
5.5.1.3 Analysis of Base Specific Cleavage Patterns 161
5.6 Applications in Quantitation of Nucleic Acids for Analysis of Gene
Expression and Gene Amplification 265
5.6.1 Analysis of DNA Mixtures and Allele Frequency Determinations in DNA
Pools 265
5.6.2 Analysis of Gene Expression 369
References 172
6 MALDI MS of Clycans 282
Dijana S*agi andjasna Peter Katalinic
6.1 Introduction 282
6.2 N Glycosylation 282
6.2.1 Release of N Glycans 284
6.2.1.1 Chemical Release 284
6.2.1.2 Enzymatic Release 284
6.2.2 Sample Preparation for MALDI MS 287
VIII I Contents
6.2.2.1 Contaminant Removal 187
6.2.2.2 Derivatization 187
6.2.3 Matrices 189
6.2.3.1 Matrices for Neutral N Glycans 189
6.2.3.2 Matrices for Acidic N Glycans 191
6.2.4 Structural Analysis 191
6.2.4.1 Fragmentation of N Glycans 191
6.2.4.2 Post Source Decay 194
6.2.4.3 Collision Induced Decomposition 195
6.2.4.4 Use of Exoglycosidase Sequencing 199
6.2.5 MALDI MS of Intact Glycoproteins 199
6.2.6 Determination of N Glycosylation Site Occupancy 201
6.3 O Glycosylation 203
6.3.1 Release of O Glycans from the Parent Protein 204
6.3.2 MALDI TOF MS of Released O Glycans 205
6.3.3 Determination of O Glycosylation Sites by PSD MALDI TOF MS 205
6.3.4 Determination of O Glycosylation Status by MALDI TOF MS 206
6.3.5 Identification of O Glycosylation in Proteins by In Gel
Alkylaminylation 206
6.3.6 O Glycoforms in Urine: Identification of O Glycosylated Amino Acids in
Mixtures by MALDI MS and Computer Assignment 207
6.3.7 Identification of the Non Covalent O Glycoprotein Dimer by Blot
IR MALDI MS 209
6.3.8 Determination of Overall O Glycosylation of a Glycoprotein by
Permethylation 209
References 210
7 MALDI MS of Lipids 215
Jurgen Schiller
7.1 Introduction 215
7.1.1 Why are Lipids of Interest? 215
7.1.2 Problems in Lipid Analysis: A Brief Comparison of Methods 217
7.1.3 Analysis of Lipids by MS 217
7.1.4 Capabilities and Limitations of MALDI TOF MS in the
Lipid Analysis 218
7.1.5 Choosing an Appropriate Matrix 219
7.1.6 Sample Preparation, Extraction and Purification 221
7.2 Analysis of Individual Lipid Classes and their Characteristics 222
7.2.1 The Apolar Lipids: Diacylglycerols, Triacylglycerols, Cholesterol and
Cholesteryl Esters 222
7.2.2 Zwitterionic Phospholipids: Sphingomyelin, Phosphatidylcholine and
Phosphatidylethanolamine 224
7.2.3 Acidic Phospholipids: Phosphatidic Acid, Cardiolipin,
Phosphatidylglycerol, Phosphatidylserine, Inositol and Higher
Phosphoinositides and their Lysolipids 227
Contents IIX
7.2.4 Free Fatty Acids 228
7.3 MALDI TOF MS of Typical Lipid Mixtures 229
7.3.1 Vegetable Oils and Frying Fats 229
7.3.2 Plant and Tissue Extracts 229
7.3.2.1 Brain Phospholipids 230
7.3.2.2 Eye Lens Phospholipids 231
7.3.2.3 Other tissues 231
7.3.3 Important Body Fluids and Cells of the Human Body 231
7.3.3.1 Blood 232
7.3.3.2 Spermatozoa and Neutrophils 232
7.3.4 Characterization of Typical Oxidation Products of Lipids 235
7.4 Quantitative Aspects of MALDI TOF MS of Lipids 236
7A.I Approaches Used To Date 236
7.5 Problems, and their Potential Solution 237
7.5.1 "Small" Molecules and Fragmentation Products 237
7.5.2 Auxiliary Reagents 238
7.6 Summary and Outlook 238
References 240
8 MALDI MS for Polymer Characterization 245
Liang Li
8.1 Introduction 245
8.2 Technical Aspects of MALDI MS 246
8.2.1 Sample Preparation Issues 246
8.2.1.1 Matrix 247
8.2.1.2 Cationization Reagent 249
8.2.1.3 Solvent 251
8.2.1.4 Solvent Free Sample Preparation 257
8.2.2 Instrumental and Measurement Issues 258
8.2.2.1 Mass Resolution and Accuracy 258
8.2.2.2 Sensitivity and Dynamic Range 263
8.2.2.3 Mass Range 267
8.2.2.4 MS/MS Capability 270
8.2.3 Data Processing Issues 273
8.3 Attributes and Limitations of MALDI MS 276
8.4 Conclusions and Perspectives 285
References 286
9 Small Molecule Desorption/lonization Mass Analysis 299
Lucinda Cohen, Eden P. Co, and Gary Siuzdak
9.1 Introduction 299
9.2 Matrix Choices for Small Molecule MALDI 300
9.2.1 Organic Matrices 300
9.2.2 Inorganic Matrices 301
9.2.3 Liquid Matrices 303
X Contents
9.2.4 Matrix Free Approaches 304
9.3 Sample Preparation 307
9.3.1 Electrospray Sample Deposition 308
9.3.2 Analyte Derivatization 308
9.3.3 Analyte Pre Concentration 309
9.3.3.1 Prestructured Sample Supports 309
9.3.3.2 DIOS with Solid Liquid Extraction 310
9.3.4 Matrix Suppression 312
9.4 Qualitative Characterization of LMM Molecules 315
9.5 Analyte Quantitation by MALDI 318
9.5.1 Selection of IS 318
9.5.2 Methods for Improving Quantitative Performance 319
9.5.3 Quantitation of Pharmaceutical Compounds 320
9.5.4 Enzyme Activity and Inhibition Studies 322
9.5.5 Quantitative Analysis of Samples from Complex Biological
Matrices 323
9.5.6 Environmental Applications of Quantitative MALDI 324
9.6 Separation Methods Coupled with MALDI and DIOS 326
9.6.1 TLC MALDI 326
9.6.2 Capillary and Frontal Affinity Liquid Chromatography 328
9.7 Conclusions 331
References 333
Index 339 |
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| discipline_str_mv | Chemie / Pharmazie Physik Biologie Chemie |
| format | Book |
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| genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content |
| genre_facet | Aufsatzsammlung |
| id | DE-604.BV021730456 |
| illustrated | Illustrated |
| index_date | 2024-07-02T15:26:16Z |
| indexdate | 2024-07-20T09:07:36Z |
| institution | BVB |
| isbn | 9783527314409 3527314407 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-014943964 |
| oclc_num | 890523555 |
| open_access_boolean | |
| owner | DE-91G DE-BY-TUM DE-19 DE-BY-UBM DE-29 DE-526 DE-29T DE-634 DE-83 DE-11 DE-188 |
| owner_facet | DE-91G DE-BY-TUM DE-19 DE-BY-UBM DE-29 DE-526 DE-29T DE-634 DE-83 DE-11 DE-188 |
| physical | XVI, 345 S. Ill., graph. Darst. 240 mm x 170 mm |
| publishDate | 2007 |
| publishDateSearch | 2007 |
| publishDateSort | 2007 |
| publisher | WILEY-VCH |
| record_format | marc |
| spelling | MALDI MS a practical guide to instrumentation, methods and applications ed. by Franz Hillenkamp ... Weinheim WILEY-VCH 2007 XVI, 345 S. Ill., graph. Darst. 240 mm x 170 mm txt rdacontent n rdamedia nc rdacarrier Espectrometría de masas Matrix-assisted laser desorption-ionization MALDI-MS (DE-588)4586449-4 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content MALDI-MS (DE-588)4586449-4 s DE-604 Hillenkamp, Franz 1936-2014 Sonstige (DE-588)106252291 oth text/html http://deposit.dnb.de/cgi-bin/dokserv?id=2843893&prov=M&dok_var=1&dok_ext=htm Inhaltstext HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=014943964&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | MALDI MS a practical guide to instrumentation, methods and applications Espectrometría de masas Matrix-assisted laser desorption-ionization MALDI-MS (DE-588)4586449-4 gnd |
| subject_GND | (DE-588)4586449-4 (DE-588)4143413-4 |
| title | MALDI MS a practical guide to instrumentation, methods and applications |
| title_auth | MALDI MS a practical guide to instrumentation, methods and applications |
| title_exact_search | MALDI MS a practical guide to instrumentation, methods and applications |
| title_exact_search_txtP | MALDI MS a practical guide to instrumentation, methods and applications |
| title_full | MALDI MS a practical guide to instrumentation, methods and applications ed. by Franz Hillenkamp ... |
| title_fullStr | MALDI MS a practical guide to instrumentation, methods and applications ed. by Franz Hillenkamp ... |
| title_full_unstemmed | MALDI MS a practical guide to instrumentation, methods and applications ed. by Franz Hillenkamp ... |
| title_short | MALDI MS |
| title_sort | maldi ms a practical guide to instrumentation methods and applications |
| title_sub | a practical guide to instrumentation, methods and applications |
| topic | Espectrometría de masas Matrix-assisted laser desorption-ionization MALDI-MS (DE-588)4586449-4 gnd |
| topic_facet | Espectrometría de masas Matrix-assisted laser desorption-ionization MALDI-MS Aufsatzsammlung |
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