Proteomics sample preparation:
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| Format: | Buch |
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| Sprache: | English |
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Weinheim
Wiley-VCH-Verl.
2008
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| Online-Zugang: | Inhaltstext Inhaltsverzeichnis |
| Beschreibung: | Literaturangaben |
| Beschreibung: | XXXII, 453 S. Ill., graph. Darst. 24 cm |
| ISBN: | 9783527317967 |
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| 245 | 1 | 0 | |a Proteomics sample preparation |c ed. by Jörg von Hagen |
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| 650 | 4 | |a Analytic Sample Preparation Methods | |
| 650 | 4 | |a Proteins |x Analysis | |
| 650 | 4 | |a Proteins |x analysis | |
| 650 | 4 | |a Proteomics | |
| 650 | 4 | |a Proteomics |x methods | |
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CONTENTS PREFACE XXI LIST OF CONTRIBUTORS XXIII LIST OF ABBREVIATIONS
XXXI PART I PERSPECTIVES IN PROTEOMICS SAMPLE PREPARATION 1 1
INTRODUCTION 3 N. LEIGH ANDERSON 2 GENERAL ASPECTS OF SAMPLE PREPARATION
FOR COMPREHENSIVE PROTEOME ANALYSIS 5 SVEN ANDRECHT ANDJORG VON HAGEN
2.1 THE NEED FOR STANDARDS IN PROTEOMICS SAMPLE PREPARATION 5 2.2
INTRODUCTION: THE CHALLENGE OF CRUDE PROTEOME SAMPLE ANALYSIS 6 2.3
GENERAL ASPECTS: PARAMETERS WHICH INFLUENCE THE SAMPLE PREPARATION
PROCEDURE 8 2.3.1 TECHNICAL DEPENDENT ASPECTS FOR SAMPLE PREPARATION IN
PROTEOMICS 9 2.3.2 SAMPLE-DEPENDENT ASPECTS FOR SAMPLE PREPARATION IN
PROTEOMICS 11 2.3.2.1 ENRICHMENT OR DEPLETION STRATEGY 11 2.3.2.2 SAMPLE
RECOVERY AND STANDARDIZATION 12 2.3.2.3 QUANTIFICATION, INTERNAL
STANDARDS AND SPIKING 13 2.3.2.4 CALCULATING THE AMOUNT OF SAMPLE FOR
PROTEOMIC APPROACHES 13 2.3.2.5 DEVELOPING PROCEDURES FOR DIFFERENT
MODEL SYSTEMS: FROM BENCH TO BEDSIDE 15 2.3.2.6 SAMPLE MATRIX 15 2.3.2.7
LOCALIZATION OF TARGET PROTEIN 1 5 2.3.3 AN EXAMPLE OF SUBCELLULAR
PROTEIN EXTRACTION 17 2.3.3.1 SUBCELLULAR EXTRACTION AND MONITORING THE
REDISTRIBUTION OF REGULATORY PROTEINS 17 PROTEOMICS SAMPLE PREPARATION.
EDITED BY JORG VON HAGEN COPYRIGHT 2008 WILEY-VCH VERLAG GMBH & CO.
KCAA, WEINHEIM ISBN: 978-3-527-31796-7 CONTENTS 2.4 SUMMARY AND
PERSPECTIVES 17 REFERENCES 19 3 PROTEOMICS: A PHILOSOPHICAL PERSPECTIVE
21 ERICH HAMBERGER 3.1 INTRODUCTION: "IN THE BEGINNING WAS THE WORD" 21
3.2 THE EXPERIMENT AS A SCIENTIFIC METHOD AND A TOOL OF COGNITION 23
3.2.1 THE EXPERIMENT HISTORICALLY VIEWED 23 3.2.2 THE EXPERIMENT
THEORETICALLY VIEWED 23 3.2.3 THE ENTANGLEMENT BETWEEN THEORY AND
EXPERIMENT 25 3.3 THE EXPERIMENT AS A METHOD (TOOL) OF COGNITION WITHIN
THE SCOPE OF BIOLOGY: THE SO-CALLED "LIFE SCIENCES" 26 3.4 PROTEOMICS AS
A COGNITION-THEORETICAL CHALLENGE 30 3.4.1 COGNITION-THEORETIC SUPPORT
FROM PHYSICS 31 3.4.2 THE "PIETSCHMANN AXIOMS" OF THE EXPERIMENT IN
BIOLOGICAL VIEW 3 2 3.5 CONCLUSION 36 REFERENCES 37 PART II METHODS 41 4
MASS SPECTROMETRY 43 4.1 A PRACTICAL GUIDELINE TO ELECTROSPRAY
IONIZATION MASS SPECTROMETRY FOR PROTEOMICS APPLICATION 43 JON BARBOUR,
SEBASTIAN WIESE, HELMUT E. MEYER, AND BETTINA WARSCHEID 4.1.1
INTRODUCTION 43 4.1.1.1 ELECTROSPRAY IONIZATION 43 4.1.1.2
NANO-ELECTROSPRAY IONIZATION 45 4.1.1.3 ESI-MS INSTRUMENTATION 45
4.1.1.4 PROTEIN IDENTIFICATION STRATEGIES 46 4.1.2 SAMPLE PREPARATION 47
4.1.2.1 PURIFICATION 48 4.1.2.2 PROTEIN DIGESTION 51 4.1.3 ESI-MS
ANALYSIS 52 4.1.3.1 PROTEIN ANALYSIS BY ESI-MS 52 4.1.3.2 PEPTIDE
ANALYSIS BY NANO-HPLC/ESI-MS 53 4.1.4 APPLICATION EXAMPLE OF ESI-MS IN
PROTEOMICS 60 4.1.5 CONCLUDING REMARKS 64 4.1.6 RECIPES AND METHODS 64
4.1.6.1 MEOH/CHLOROFORM PROTEIN PRECIPITATION TO REMOVE SALTS AND
DETERGENTS 64 4.1.6.2 PREPARATION AND WASHING OF A CRUDE MEMBRANE PELLET
6 5 4.1.6.3 PROTEOLYTIC DIGESTION AND PEPTIDE EXTRACTION 65 IX 4.1.6.4
OFF-LINE ANALYSIS OF INTACT PROTEINS 6/ 4.1.6.5 ESI SAMPLE PREPARATION
CHECKLIST 67 REFERENCES 68 4.2 SAMPLE PREPARATION FOR THE APPLICATION OF
MALDI MASS SPECTROMETRY IN PROTEOME ANALYSIS 73 ANDREAS THOLEY, MATTHIAS
GLUCKMANN, KERSTIN SEEMANN, AND MICHAEL KARAS 4.2.1 INTRODUCTION 73
4.2.2 SAMPLE PREPARATION FOR MALDI-BASED PROTEIN IDENTIFICATION 75
4.2.2.1 SELECTION OF THE MALDI MATRIX 75 4.2.3 SAMPLE PREPARATION 78
4.2.4 LC-MALDI 84 4.2.5 APPLICATION EXAMPLE 85 4.2.5.1 GEL-BASED
WORKFLOW 85 4.2.5.2 APPLICATION EXAMPLE: LC-MALDI WORKFLOW 87 4.2.6
SUMMARY 88 4.2.7 PERSPECTIVES 89 4.2.8 RECIPES FOR BEGINNERS 90 4.2.8.1
SAMPLE SPOTTING TECHNIQUES 90 4.2.8.2 SAMPLE CLEANING PROCEDURES 90
REFERENCES 91 4.3 SAMPLE PREPARATION FOR LABEL-FREE PROTEOMIC ANALYSES
OF BODY FLUIDS BY FOURIER TRANSFORM ION CYCLOTRON MASS SPECTROMETRY 95
CLOUD P. PAWELETZ, NATHAN A. YATES, AND RONALD C. HENDRICKSON 4.3.1
INTRODUCTION 95 4.3.2 PERSPECTIVE 99 4.3.3 RECIPE FOR BEGINNERS 100
4.3.3.1 STEP-BY-STEP INSTRUCTIONS 102 REFERENCES 103 4.4 SAMPLE
PREPARATION FOR DIFFERENTIAL PROTEOME ANALYSIS: LABELING TECHNOLOGIES
FOR MASS SPECTROMETRY 105 JOSEF KELLERMANN 4.4.1 INTRODUCTION 105 4.4.2
ISOTOPIC LABELING OF PEPTIDES AND/OR PROTEINS 107 4.4.2.1 STABLE ISOTOPE
LABELING OF PROTEINS IN CELL CULTURE 107 4.4.2.2 CHEMICAL ISOTOPIC
LABELING OF PEPTIDES OR PROTEINS 108 4.4.2.3 SPIKING OF LABELED PEPTIDES
111 4.4.3 SUMMARY 111 4.4.4 PERSPECTIVES 112 4.4.5 RECIPE FOR BEGINNERS
112 REFERENCES 114 X CONTENTS 4.5 DETERMINING MEMBRANE PROTEIN
LOCALIZATION WITHIN SUBCEILULAR COMPARTMENTS USING STABLE ISOTOPE
TAGGING 118 KATHRYN S. LI HEY, TOM DUNKLEY, AND PAWE! SADOWSKI 4.5.1
INTRODUCTION 118 4.5.2 PREPARATION AND TREATMENT OF SAMPLES IN THE
EARLY-STAGE LOPIT PROTOCOL 120 4.5.2.1 PREPARATION AND FRACTIONATION OF
ORGANELLES 120 4.5.2.2 CARBONATE WASHING OF FRACTIONS TO LYSE
ORGANELLES, AND REMOVAL OF SOLUBLE AND PERIPHERAL PROTEINS 123 4.5.2.3
ITRAQ LABELING 124 4.5.3 APPLICATION OF LOPIT TO MAP THE ORGARIELLE
PROTEOME OF ARABIDOPSIS 125 4.5.4 SUMMARY 126 4.5.5 RECIPE FOR BEGINNERS
127 REFERENCES 127 5 ELECTROPHORESIS 129 5.1 SAMPLE PREPARATION FOR
TWO-DIMENSIONAL GEL ELECTROPHORESIS 129 WALTER WEISS AND ANGELIKA CORG
5.1.1 INTRODUCTION 129 5.1.2 GENERAL ASPECTS OF SAMPLE PREPARATION FOR
2-DGE 130 5.1.2.1 CELL DISRUPTION 130 5.1.2.2 SAMPLE CLEAN-UP 132
5.1.2.3 PROTEIN SOLUBILIZATION 135 5.1.3 APPLICATION SAMPLES 137 5.1.3.1
MAMMALIAN TISSUES 138 5.1.3.2 MICROBIAL CELL CULTURES 138 5.1.3.3 PLANT
CELLS 138 5.1.4 SUMMARY 139 5.1.5 PERSPECTIVE 140 5.1.6 RECIPES FOR
BEGINNERS 141 REFERENCES 142 5.2 SAMPLE PREPARATION FOR NATIVE
ELECTROPHORESIS 144 ILKA WITTIG AND HERMANN SCHAGGER 5.2.1 INTRODUCTION
144 5.2.2 SAMPLE PREPARATION: GENERAL CONSIDERATIONS 146 5.2.2.1 CHOICE
OF DETERGENT AND DETERGENT/PROTEIN RATIO 146 5.2.2.2 CHOICE OF IONIC
STRENGTH AND PH FOR SAMPLE SOLUBILIZATION 147 5.2.2.3 STORAGE OF
BIOLOGICAL MEMBRANES 148 5.2.2.4 EFFECTS OF ADDING COOMASSIE DYE TO
SAMPLE AND/OR CATHODE BUFFER FOR BNE 149 5.2.3 APPLICATIONS 150 5.2.3.1
SOLUBILIZATION OF BACTERIAL MEMBRANES, YEAST AND MAMMALIAN MITOCHONDRIA
250 CONTENTS \ X! 5.2.3.2 HOMOGENIZATION AND SOLUBIIIZATION OF MAMMALIAN
CELLS AND TISSUES 150 5.2.3.3 RECIPE FOR BEGINNERS: MASS CALIBRATION
LADDER FOR BNE 151 5.2.4 SUMMARY AND PERSPECTIVES 151 REFERENCES 152 5.3
SAMPLE PREPARATION FOR LC-MS/MS USING FREE-FLOW ELECTROPHORESIS 155
MIKKE! NISSUM, AFICMEH ABDOLZADE-BAVIL, SAB'ME KUHFUSS, ROBERT
WILDGRUBER, GERHARD WEBER, AND CHRISTOPH ECKERSKOM 5.3.1 INTRODUCTION
155 5.3.2 THE PROBLEMS OF SAMPLE PREPARATION: THE PROS AND CONS 157
5.3.2.1 SEPARATION 157 5.3.2.2 EXTRACTION 158 5.3.2.3 MEDIA COMPOSITION
158 5.3.3 APPLICATION EXAMPLE 159 5.3.3.1 REAGENTS 159 5.3.3.2 SAMPLE
PREPARATION FOR FFE 160 5.3.3.3 FFE SEPARATION OF PEPTIDES 160 5.3.3.4
RPLC-MS/MS ANALYSIS 161 5.3.3.5 DATA PROCESSING 161 5.3.4 SUMMARY 161
5.3.5 PERSPECTIVE 165 5.3.6 RECIPE FOR BEGINNERS 166 5.3.6.1 FFE SET-UP
PROCEDURE 166 5.3.6.2 PRE-EXPERIMENTAL QUALITY CONTROL (QC) 167 5.3.6.3
EXPERIMENT 168 REFERENCES 168 5.4 SAMPLE PREPARATION FOR CAPILLARY
ELECTROPHORESIS 171 ROSS BURN AND DAVID PERRETT 5.4.1 INTRODUCTION 171
5.4.2 SAMPLE PREPARATION 173 5.4.2.1 SAMPLE COLLECTION AND STORAGE 174
5.4.2.2 SAMPLE PREPARATION FOR CE 174 5.4.2.3 SAMPLE CONCENTRATION 175
5.4.2.4 OFF-LINE PRECONCENTRATION 275 5.4.2.5 ON-LINE PRECONCENTRATION
175 5.4.2.6 DESALTING 176 5.4.2.7 ANALYTE MODIFICATION 176 5.4.3
BACKGROUND ELECTROLYTE 277 5.4.4 CAPILLARY PREPARATION 178 5.4.4.1
CAPILLARY DIMENSIONS 178 5.4.4.2 CAPILLARY CONDITIONING 178 5.4.4.3
CAPILLARY COATING 179 5.4.5 SUMMARY 179 XII CONTENTS 5.4.6 PERSPECTIVE
179 5.4.7 RECIPE FOR BEGINNERS 180 5.4.7.1 METHOD 1: ANALYSIS OF HUMAN
SERUM/PLASMA BY C2E 180 5.4.7.2 METHOD 2: ANALYSIS OF TRYPTIC DIGESTS BY
CZE 282 5.4.7.3 METHOD 3: ANALYSIS OF PROTEOMES BY CIEF 183 REFERENCES
185 6 OPTICAL METHODS 187 6.1 HIGH-THROUGHPUT PROTEOMICS: SPINNING DISC
INTERFEROMETRY (SDI) 187 PATRICIO ESPINOZA VALLEJOS, GREG LAWRENCE,
DAVID NOLTE, FRED REGNIER, AND JOERG SCHREIBER 6.1.1 PROTEOMICS AS A
TOOL FOR HEALTH ASSESSMENT 287 6.1.2 TRANSLATIONAL PROTEOMICS 188 6.1.3
THE PRINCIPLES OF SPINNING DISC INTERFEROMETRY 189 6.1.3.1 THE SPINNING
DISC 289 6.1.3.2 WHY SPIN? 191 6.1.3.3 IN-LINE QUADRATURE 292 6.1.3.4
SCALING MASS SENSITIVITY 194 6.1.4 THE SPINNING DISC AS A
HIGH-THROUGHPUT IMMUNOLOGICAL ASSAY PLATFORM 2 96 6.1.4.1 IMMUNOLOGICAL
ASSAYS USING A DISC ARRAY FORMAT 297 6.1.4.2 ASSAY FORMATS 298 6.1.4.3
ASSAY PROTOCOLS 299 6.1.5 TYPES OF ASSAY THAT FIT THE SPINNING DISC 200
6.1.5.1 ASSAY STRUCTURE 200 6.1.5.2 ASSAY DEVELOPMENT KIT (ADK) 202
6.1.6 ASSAY AND SAMPLE PROCESSING 202 6.1.6.1 HIGH-THROUGHPUT SYSTEM 201
6.1.6.2 THE ADK 203 6.1.7 CONCLUSIONS 205 REFERENCES 206 6.2 OPTICAL
PROTEOMICS ON CELL ARRAYS 208 ANDREAS QROD AND PHILIPPE BASTIAENS
INTRODUCTION 208 A DESCRIPTION OF THE PROBLEM WITH REGARDS TO SAMPLE
PREPARATION 22 2 GENERAL REMARKS 22 2 CELL LINE SELECTION 222 SAMPLE
PREPARATION 222 CHOICE OF TRANSFECTION REAGENT 222 NUCLEIC ACID
PREPARATION 223 SAMPLE SCALE: HOW MANY DUPLICATES ARE REQUIRED? 223
CHOICE OF MICROARRAYER/MICROSPOTTING SYSTEM (SPOTTER) 223 LAYOUT DESIGN
(SPOTTING PATTERN) 224 6.2. 6.2. .1 .2 6.2.2.1 6.2.2.2 6.2. 6.2. 6.2.
6.2. 6.2. 6.2. .2.3 .2.4 .2.5 .2.6 .2.7 .2.8 CONTENTS XII! 6.2.3 SUMMARY
215 6.2.4 PERSPECTIVES 235 6.2.5 SAMPLE PREPARATION: SHORT PROTOCOL 215
6.2.5.1 RECOMMENDED EQUIPMENT AND CONSUMABLES 215 6.2.5.2 PREPARATION OF
THE SOURCE PLATE 216 6.2.5.3 SPOTTING 217 6.2.5.4 CELL CULTURE AND
EXPERIMENT 217 REFERENCES 218 6.3 SAMPLE PREPARATION BY LASER
MICRODISSECTION AND CATAPULTING FOR PROTEOME ANALYSIS 219 KARIN SCHUTZE,
ANDREA BUCHSTALLER, YILMAZ NIYAZ, CHRISTIAN MELLE, CUNTHER ERNST,
KERSTIN DAVID, THORSTEN SCHLOMM, AND FERDINAND VON EGGELING 6.3.1
INTRODUCTION: LASER MICRODISSECTION AND FUNCTIONAL PROTEOMIC RESEARCH
219 6.3.2 THE RELEVANCE OF PURE STARTING MATERIAL FOR PROTEOMICS 219
6.3.3 EXAMPLES OF COMBINED LMPC AND PROTEOMIC ANALYSES 220 6.3.3.1 LMPC
AND PREECLAMPSIA 220 6.3.3.2 LMPC AND RENAL CELL CARCINOMA 221 6.3.3.3
LMPC AND HEPATOCELLULAR CARCINOMA 221 6.3.3.4 LMPC AND BRAIN DISORDERS
221 6.3.3.5 LMPC AND PLANT BIOLOGY 221 6.3.4 LMPC ADAPTED FOR PROTEOMIC
APPLICATIONS 222 6.3.5 LMPC COMBINED WITH SELDI-TOF MS: A PROMISING
APPROACH FOR PATIENT-SPECIFIC ANALYSES 224 6.3.6 CORRELATION OF GENE AND
PROTEIN EXPRESSION: THE BEST DATA CAPTURE FOR COMPREHENSIVE DIAGNOSIS
228 6.3.7 RECIPE FOR BEGINNERS 228 6.3.7.1 PATIENTS AND SPECIMENS 228
6.3.7.2 LASER MICRODISSECTION OF TISSUE SECTIONS 230 6.3.7.3 PROTEINCHIP
ARRAY PREPARATION AND ANALYSIS 230 6.3.8 SUMMARY AND OUTLOOK 231
REFERENCES 232 6.4 SAMPLE PREPARATION FOR FLOW CYTOMETRY 234 DEREK C. DA
VIES 6.4.1 I NTR ODUCTIO N 234 6.4.2 SAMPLE PREPARATION FOR FLOW
CYTOMETRY 236 6.4.2.1 PREPARATION FROM CELLS IN SUSPENSION 236 6.4.2.2
PREPARATION FROM ADHERENT CELLS 237 6.4.2.3 PREPARATION FROM SOLID
TISSUE 237 6.4.2.4 GENERAL CONSIDERATIONS 237 6.4.3 IDENTIFICATION OF
RELEVANT CELLS 238 6.4.4 CELL SORTING 238 6.4.4.1 CELLS AND SAMPLES 238
6.4.4.2 CYTOMETER CONSIDERATIONS 239 XIV CONTENTS 6.4.5 APPLICATION
EXAMPLE 240 6.4.6 SUMMARY 242 6.4.7 PERSPECTIVES 242 6.4.8 RECIPES FOR
BEGINNERS 242 6.4.8.1 CULTURED SUSPENSION CELLS 242 6.4.8.2 ADHERENT
CELLS 242 6.4.8.3 SOLID TISSUE 243 REFERENCES 243 7 CHROMATOGRAPHY 245
7.1 SAMPLE PREPARATION FOR HPLC-BASED PROTEOME ANALYSIS 245 EGIDIJUS
MACHTEJEVAS AND KLAUS K. LINGER 7.1.1 INTRODUCTION 245 7.1.2 PROBLEMS
RELATED TO DIRECT SAMPLE INJECTION IN HPLC 246 7.1.3 TRIAL AND ERROR
SELECTION OF THE SAMPLE PREPARATION METHOD 247 7.1.4 CLASSICAL
APPROACHES 249 7.1.5 SPECIFIC APPROACHES APPLIED TO SAMPLE CLEAN-UP IN
PROTEOMICS 250 7.1.5.1 MINIATURIZED EXTRACTION TECHNIQUES 250 7.1.5.2
MOST ABUNDANT COMPONENT DEPLETION 250 7.1.5.3 AFFINITY-ENRICHMENT
APPROACHES 251 7.1.6 ON-LINE SAMPLE CLEAN-UP APPROACHES 252 I.X.I
RESTRICTED ACCESS TECHNOLOGY 254 7.1.8 APPLICATION EXAMPLE: THE CASE
STUDY 259 7.1.9 CONCLUSION AND PERSPECTIVES 260 REFERENCES 262 7.2
SAMPLE PREPARATION FOR TWO-DIMENSIONAL PHOSPHOPEPTIDE MAPPING AND
PHOSPHOAMINO ACID ANALYSIS 265 ANAMARIJA KRULJAC-LETUNIC AND ANDREE
BLAUKAT 7.2.1 INTRODUCTION 265 7.2.2 IMPORTANT ASPECTS IN SAMPLE
PREPARATION PROCEDURES 265 7.2.3 APPLICATION EXAMPLE 267 7.2.4 SUMMARY
267 7.2.5 PERSPECTIVE 269 7.2.6 RECIPE FOR BEGINNERS 269 7.2.6.1 2-D
PHOSPHOPEPTIDE MAPPING PROCEDURE 269 7.2.6.2 PHOSPHOAMINO ACID ANALYSIS
PROCEDURE 271 REFERENCES 271 8 STRUCTURAL PROTEOMICS 273 8.1 EXPLORING
PROTEIN-LIGAND INTERACTIONS BY SOLUTION NMR 273 RUDOLF HARTMANN, THOMAS
STANGLER, BERND W.KONIG, AND DIETER WILLBOLD 8.1.1 INTRODUCTION 273
8.1.2 LOCALIZATION OF INTERACTION SITES BY CHEMICAL SHIFT PERTURBATION
(CSP) MAPPING 274 CONTENTS XV 8.1.3 SATURATION TRANSFER DIFFERENCE
SPECTROSCOPY 276 8.1.4 LIGAND SCREENING BY NMR 278 REFERENCES 2,79 8.2
SAMPLE PREPARATION FOR CRYSTALLOGRAPHY 281 DJORDJE MUSIL INTRODUCTION
281 USE OF RECOMBINANT PROTEINS IN CRYSTALLIZATION 282 PROTEIN
SOLUBILITY AND CRYSTALLIZATION 284 PROTEIN CRYSTALLIZATION 286 PRACTICAL
EXAMPLES 291 REFERENCES 292 INTERACTION ANALYSIS 295 SAMPLE PREPARATION
FOR PROTEIN COMPLEX ANALYSIS BY THE TANDEM AFFINITY PURIFICATION (TAP)
METHOD 295 BERTRAND SERAPHIM AND ANDRZEJ DZIEMBOWSKI INTRODUCTION 295
THE PROBLEM WITH REGARDS TO SAMPLE PREPARATION: THE PROS AND THE CONS
296 APPLICATION EXAMPLE 300 SUMMARY 301 PERSPECTIVE 301 RECIPE FOR
BEGINNERS 301 REFERENCES 302 9.2 EXPLORING MEMBRANE PROTEOMES 303
FILIPPA STENBERG AND DANIEL O. DALEY 9.2.1 INTRODUCTION 303 9.2.2
DENNING MEMBRANE PROTEOMES 303 9.2.3 SEPARATION OF MEMBRANE PROTEOMES
304 9.2 A EXPERIMENTAL IDENTIFICATION OF MEMBRANE PROTEINS 307 9.2.5
MAPPING MEMBRANE INTERACTOMES 307 9.2.6 STRUCTURAL ANALYSIS OF MEMBRANE
PROTEOMES 308 9.2.7 SUMMARY AND PERSPECTIVE 309 9.2.8 RECIPE FOR
BEGINNERS 311 9.2.8.1 SAMPLE PREPARATION 311 9.2.8.2 BN-PAGE 311 9.2.8.3
SDS-PAGE 312 REFERENCES 312 10 POST-TRANSLATIONAL MODIFICATIONS 317 10.1
SAMPLE PREPARATION FOR PHOSPHOPROTEOME ANALYSIS 317 RENE P. ZAHEDI AND
ALBERT SICKMANN 10.1.1 INTRODUCTION 317 10.1.2 GENERAL SAMPLE
PREPARATION 317 8.2 .1 8.2.2 8.2 8.2 8.2 9 9.1 9.1 9.1 9.1 9.1 9.1 9.1
.3 .4 .5 .1 .2 .3 .4 .5 .6 XVI CONTENTS 10.1.3 REDUCTION OF SAMPLE
COMPLEXITY 318 10.13.1 GEL ELECTROPHORESIS 318 10.1.3.2 ISOELECTRIC
FOCUSING 318 10.1.4 METHODS FOR PHOSPHOPEPTIDE/PROTEIN ENRICHMENT 319
10.1.4.1 IMMUNOPRECIPITATION 319 10.1.4.2 IMMOBILIZED METAL ION AFFINITY
CHROMATOGRAPHY (IMAC) 319 10.1.4.3 METAL OXIDES 320 10.1.4.4
CATION-EXCHANGE CHROMATOGRAPHY 321 10.1.4.5 DERIVATIZATION APPROACHES
322 10.1.5 SUMMARY 323 10.1.6 PERSPECTIVE 324 10.1.7 RECIPE FOR
BEGINNERS: IMAC 324 REFERENCES 325 10.2 SAMPLE PREPARATION FOR ANALYSIS
OF POST-TRANSLATIONAL MODIFICATIONS: GLYCOSYLATION 328 DAVID S. SELBY,
MARTIN R. LARSEN, MIRENJ. OMAETXEHARRIA, AND PETER ROEPSTORJF 10.2.1
INTRODUCTION 328 10.2.2 ADVANTAGES AND DISADVANTAGES OF DIFFERENT SAMPLE
PREPARATION METHODS 331 10.2.3 EXAMPLE APPLICATIONS OF ENRICHMENT
METHODS 334 10.2.3.1 ZIC-HILIC MICROCOLUMNS FOR PREPARATION OF N-LINKED
GLYCAN-CONTAINING SAMPLES 334 10.2.3.2 TITANIUM DIOXIDE MICROCOLUMNS FOR
ENRICHMENT OF SIALIC ACID-CONTAINING GLYCOPEPTIDES AND
GLYCOSYLPHOSPHATIDYLINOSITOL LIPID-ANCHORED PEPTIDES 336 10.2.4 SUMMARY
337 10.2.5 PERSPECTIVE 338 10.2.6 RECIPE FOR BEGINNERS: ENRICHMENT OF
GLYCOPEPTIDES WITH A HILIC MICROCOLUMN 338 10.2.6.1 MATERIALS 338
10.2.6.2 PROCEDURE: PURIFICATION OF GLYCOPEPTIDES 339 10.2.6.3
PROCEDURE: DEGLYCOSYLATION OF N-LINKED GLYCOPEPTIDES 339 REFERENCES 340
11 SPECIES-DEPENDENT PROTEOMICS 343 11.1 SAMPLE PREPARATION AND DATA
PROCESSING IN PLANT PROTEOMICS 343 KATJA BAERENFALLER, WILHELM GRUISSEM,
AND SACHA BAGINSKY 11.1.1 INTRODUCTION 343 1.1.1.2 PLANT-SPECIFIC
CONSIDERATIONS IN PROTEOMICS 344 11.1.2.1 CELL WALLS 344 11.1.2.2
PLASTIDS 344 11.1.2.3 PROTEIN EXTRACTION FROM PLANT TISSUE 345 11.1.2.4
EXTRACTION FROM RECALCITRANT AND RESISTANT TISSUE 345 XVI! 11.1.2.5
DYNAMIC RANGE LIMITATIONS 346 11.1.2.6 PROTEORNICS IN AS-YEL UNSEQUENCED
ORGANISMS 346 11.1.3 SAMPLE PREPARATION PROTOCOLS 347 11.13.1 CEIL WAIL
PROTEIN EXTRACTION 348 11.13.2 PLASTIC! ISOLATION 349 11.1.3.3 PROTEIN
EXTRACTION WITH TCA/ ACETONE 350 11.1.3.4 PHENOL EXTRACTION 35 1
11.1.3.5 SERIAL EXTRACTION 351 11.1.3.6 EXTRACTION FROM RECALCITRANT AND
RESISTANT TISSUE 352 11.1.3.7 EXTRACTION AND FRACTIONATION WITH
POLYETHYLENE GLYCOL (PEG) 353 11.1.3.8 STAGES FOLLOWING PROTEIN
EXTRACTION 353 11.1.4 MS/MS DATA PROCESSING FOR UNSEQUENCED ORGANISMS
354 11.1.5 CONCLUDING REMARKS 355 REFERENCES 356 11.2 SAMPLE PREPARATION
FOR MUDPIT WITH BACTERIAL PROTEIN SAMPLES 358 ANSGAR POETSCH AND DIRK
WOLTERS 11.2.1 INTRODUCTION 358 11.2.2 THE MUDPIT TECHNOLOGY 359 11.2.3
MEMBRANE PROTEINS AND MUDPIT 361 11.2.4 QUANTITATIVE MUDPIT 363 11.2.5
LIMITATIONS OF MUDPIT 364 11.2.6 PITFALLS OF MUDPIT 365 11.2.7 SUMMARY
365 11.2.8 PERSPECTIVE 365 11.2.9 RECIPE FOR BEGINNERS: MUDPIT: SOLUBLE
AND MEMBRANE PROTEINS 366 REFERENCES 368 11.3 SAMPLE PREPARATION FOR THE
CELL-WALL PROTEOME ANALYSIS OF YEAST AND FUNGI 371 KAI SOHN, EKKEHARD
HITLER, AND STEFFEN RUPP 11.3.1 INTRODUCTION 371 113.2 DESCRIPTION OF
THE PROBLEM WITH REGARDS TO SAMPLE PREPARATION 372 11.3.3 APPLICATION
EXAMPLE 373 11.3.4 SUMMARY 375 11.3.5 PERSPECTIVE 376 11.3.6 RECIPE FOR
BEGINNERS 376 113.6.1 CULTURES 376 113.6.2 PREPARATION OF SOLUBLE
CELL-SURFACE PROTEINS 376 113.6.3 PREPARATION OF PEPTIDES FROM
COVALENTLY LINKED CELL-WALL PROTEINS 377 REFERENCES 378 12 THE HUMAN
PROTEOSOME 379 12.1 CLINICAL PROTEOMICS: SAMPLE PREPARATION AND
STANDARDIZATION 379 GERD SCHMITZ AND CARSTEN GNEWUCH 12.1.1 INTRODUCTION
379 XVIII CONTENTS 12.1.2 THE PREANALYTICAL PHASE: SAMPLE PREPARATION,
STANDARDIZATION, AND QUALITY MANAGEMENT 380 12.1.2.1 STANDARDIZATION OF
THE (PRE)-ANALYTICAL PROCESS 381 12.1.3 PROTEOMICS IN BODY FLUIDS 382
12.1.3.1 TECHNIQUES FOR PROTEOMIC ANALYSIS 382 12.1.3.2 APPLICATIONS 383
12.1.3.3 PREPARATION OF CLINICAL SAMPLES FOR FLUIDIC PROTEOMICS 386
12.1.4 CELLULAR PROTEOMICS (CYTOMICS) 389 12.1.4.1 SAMPLE PREPARATION
AND STANDARDIZATION FOR CLINICAL CYTOMICS 389 12.1.4.2 TISSUE ARRAYS 390
12.1.4.3 BEAD-BASED IMMUNOASSAYS FOR PROTEIN ANALYSIS 391 12.1.4.4
PREPARATIVE METHODS 391 12.1.4.5 CLINICAL APPLICATIONS IN CYTOMICS 399
12.1.5 CONCLUSION 404 REFERENCES 405 12.2 STERN CELL PROTEOMICS 412
REGINA EBERT, GABRIELE MOLLER, JERZY ADAMSKI, AND FRANZ JAKOB 12.2.1
INTRODUCTION 412 12.2.2 STEM CELL NICHES 413 12.2.3 WHY STUDY PROTEOMES
IN STEM CELLS? 413 12.2.4 TECHNICAL CHALLENGES AND PROBLEMS 414 12.2.4.1
STEM CELL PREPARATION 414 12.2.4.2 CULTIVATION 415 12.2.4.3 TREATMENT
415 12.2.4.4 WHOLE-CELL PROTEOME 415 12.2.4.5 SECRETORY PROTEOME 425
12.2.5 RECIPES FOR BEGINNERS 417 12.2.5.1 WHOLE-CELL LYSATE 417 12.2.5.2
SECRETORY PROTEOME PROCEDURE 418 12.2.5.3 LABELING WITH 35 S 418
12.2.5.4 ETHANOL PRECIPITATION 419 12.2.5.5 TCA PRECIPITATION 4 1 9
REFERENCES 419 13 BIOINFORMATICS 423 13.1 BIOINFORMATICS SUPPORT FOR
MASS SPECTROMETRIC QUALITY CONTROL 423 KNUT REINERT, TIM CONRAD, AND
OLIVER KOHLBACHER 13.1.1 INTRODUCTION 423 13.1.2 PROBLEM DESCRIPTION 423
13.1.2.1 SIGNAL PROCESSING PITFALLS 424 13.1.2.2 MAP QUALITY CONTROL 425
13.1.2.3 STATISTICAL VALIDATION RESULTS 425 13.1.3 QUALITY ASSESSMENT
FOR ONE-DIMENSIONAL (1-D) MS DATA 426 13.1.3.1 FILTER 427 CONTENTS I XIX
13.1.4 APPLICATION EXAMPLE; ABSOLUTE QUANTIFICATION OF AN UNKNOWN
PEPTIDE CONTENT 428 13.1.5 SUMMARY 429 13.1.6 PERSPECTIVE 430 13.1.7
RECIPE FOR BEGINNERS 430 13.1.7.1 ACQUIRING THE RA W DATA 430 13.1.7.2
PREPROCESSING THE DATA 431 13.1.7.3 ANALYZING THE PREPROCESSED DATA 431
REFERENCES 431 13.2 USE OF PHYSICO-CHEMICAL PROPERTIES IN PEPTIDE AND
PROTEIN IDENTIFICATION 433 ANASTASIA K. YOCUM, PETERJ. ULINTZ, AND
PHILIP C. ANDREWS 13.2.1 INTRODUCTION 433 13.2.2 ISOELECTRIC POINT 434
13.2.3 ION-EXCHANGE CHROMATOGRAPHY 436 13.2.4 REVERSED-PHASE
CHROMATOGRAPHY 438 13.2.5 MASS ACCURACY 442 13.2.6 SUMMARY 443
REFERENCES 444 INDEX 449 |
| adam_txt |
CONTENTS PREFACE XXI LIST OF CONTRIBUTORS XXIII LIST OF ABBREVIATIONS
XXXI PART I PERSPECTIVES IN PROTEOMICS SAMPLE PREPARATION 1 1
INTRODUCTION 3 N. LEIGH ANDERSON 2 GENERAL ASPECTS OF SAMPLE PREPARATION
FOR COMPREHENSIVE PROTEOME ANALYSIS 5 SVEN ANDRECHT ANDJORG VON HAGEN
2.1 THE NEED FOR STANDARDS IN PROTEOMICS SAMPLE PREPARATION 5 2.2
INTRODUCTION: THE CHALLENGE OF CRUDE PROTEOME SAMPLE ANALYSIS 6 2.3
GENERAL ASPECTS: PARAMETERS WHICH INFLUENCE THE SAMPLE PREPARATION
PROCEDURE 8 2.3.1 TECHNICAL DEPENDENT ASPECTS FOR SAMPLE PREPARATION IN
PROTEOMICS 9 2.3.2 SAMPLE-DEPENDENT ASPECTS FOR SAMPLE PREPARATION IN
PROTEOMICS 11 2.3.2.1 ENRICHMENT OR DEPLETION STRATEGY 11 2.3.2.2 SAMPLE
RECOVERY AND STANDARDIZATION 12 2.3.2.3 QUANTIFICATION, INTERNAL
STANDARDS AND SPIKING 13 2.3.2.4 CALCULATING THE AMOUNT OF SAMPLE FOR
PROTEOMIC APPROACHES 13 2.3.2.5 DEVELOPING PROCEDURES FOR DIFFERENT
MODEL SYSTEMS: FROM BENCH TO BEDSIDE 15 2.3.2.6 SAMPLE MATRIX 15 2.3.2.7
LOCALIZATION OF TARGET PROTEIN 1 5 2.3.3 AN EXAMPLE OF SUBCELLULAR
PROTEIN EXTRACTION 17 2.3.3.1 SUBCELLULAR EXTRACTION AND MONITORING THE
REDISTRIBUTION OF REGULATORY PROTEINS 17 PROTEOMICS SAMPLE PREPARATION.
EDITED BY JORG VON HAGEN COPYRIGHT 2008 WILEY-VCH VERLAG GMBH & CO.
KCAA, WEINHEIM ISBN: 978-3-527-31796-7 CONTENTS 2.4 SUMMARY AND
PERSPECTIVES 17 REFERENCES 19 3 PROTEOMICS: A PHILOSOPHICAL PERSPECTIVE
21 ERICH HAMBERGER 3.1 INTRODUCTION: "IN THE BEGINNING WAS THE WORD" 21
3.2 THE EXPERIMENT AS A SCIENTIFIC METHOD AND A TOOL OF COGNITION 23
3.2.1 THE EXPERIMENT HISTORICALLY VIEWED 23 3.2.2 THE EXPERIMENT
THEORETICALLY VIEWED 23 3.2.3 THE ENTANGLEMENT BETWEEN THEORY AND
EXPERIMENT 25 3.3 THE EXPERIMENT AS A METHOD (TOOL) OF COGNITION WITHIN
THE SCOPE OF BIOLOGY: THE SO-CALLED "LIFE SCIENCES" 26 3.4 PROTEOMICS AS
A COGNITION-THEORETICAL CHALLENGE 30 3.4.1 COGNITION-THEORETIC SUPPORT
FROM PHYSICS 31 3.4.2 THE "PIETSCHMANN AXIOMS" OF THE EXPERIMENT IN
BIOLOGICAL VIEW 3 2 3.5 CONCLUSION 36 REFERENCES 37 PART II METHODS 41 4
MASS SPECTROMETRY 43 4.1 A PRACTICAL GUIDELINE TO ELECTROSPRAY
IONIZATION MASS SPECTROMETRY FOR PROTEOMICS APPLICATION 43 JON BARBOUR,
SEBASTIAN WIESE, HELMUT E. MEYER, AND BETTINA WARSCHEID 4.1.1
INTRODUCTION 43 4.1.1.1 ELECTROSPRAY IONIZATION 43 4.1.1.2
NANO-ELECTROSPRAY IONIZATION 45 4.1.1.3 ESI-MS INSTRUMENTATION 45
4.1.1.4 PROTEIN IDENTIFICATION STRATEGIES 46 4.1.2 SAMPLE PREPARATION 47
4.1.2.1 PURIFICATION 48 4.1.2.2 PROTEIN DIGESTION 51 4.1.3 ESI-MS
ANALYSIS 52 4.1.3.1 PROTEIN ANALYSIS BY ESI-MS 52 4.1.3.2 PEPTIDE
ANALYSIS BY NANO-HPLC/ESI-MS 53 4.1.4 APPLICATION EXAMPLE OF ESI-MS IN
PROTEOMICS 60 4.1.5 CONCLUDING REMARKS 64 4.1.6 RECIPES AND METHODS 64
4.1.6.1 MEOH/CHLOROFORM PROTEIN PRECIPITATION TO REMOVE SALTS AND
DETERGENTS 64 4.1.6.2 PREPARATION AND WASHING OF A CRUDE MEMBRANE PELLET
6 5 4.1.6.3 PROTEOLYTIC DIGESTION AND PEPTIDE EXTRACTION 65 IX 4.1.6.4
OFF-LINE ANALYSIS OF INTACT PROTEINS 6/ 4.1.6.5 ESI SAMPLE PREPARATION
CHECKLIST 67 REFERENCES 68 4.2 SAMPLE PREPARATION FOR THE APPLICATION OF
MALDI MASS SPECTROMETRY IN PROTEOME ANALYSIS 73 ANDREAS THOLEY, MATTHIAS
GLUCKMANN, KERSTIN SEEMANN, AND MICHAEL KARAS 4.2.1 INTRODUCTION 73
4.2.2 SAMPLE PREPARATION FOR MALDI-BASED PROTEIN IDENTIFICATION 75
4.2.2.1 SELECTION OF THE MALDI MATRIX 75 4.2.3 SAMPLE PREPARATION 78
4.2.4 LC-MALDI 84 4.2.5 APPLICATION EXAMPLE 85 4.2.5.1 GEL-BASED
WORKFLOW 85 4.2.5.2 APPLICATION EXAMPLE: LC-MALDI WORKFLOW 87 4.2.6
SUMMARY 88 4.2.7 PERSPECTIVES 89 4.2.8 RECIPES FOR BEGINNERS 90 4.2.8.1
SAMPLE SPOTTING TECHNIQUES 90 4.2.8.2 SAMPLE CLEANING PROCEDURES 90
REFERENCES 91 4.3 SAMPLE PREPARATION FOR LABEL-FREE PROTEOMIC ANALYSES
OF BODY FLUIDS BY FOURIER TRANSFORM ION CYCLOTRON MASS SPECTROMETRY 95
CLOUD P. PAWELETZ, NATHAN A. YATES, AND RONALD C. HENDRICKSON 4.3.1
INTRODUCTION 95 4.3.2 PERSPECTIVE 99 4.3.3 RECIPE FOR BEGINNERS 100
4.3.3.1 STEP-BY-STEP INSTRUCTIONS 102 REFERENCES 103 4.4 SAMPLE
PREPARATION FOR DIFFERENTIAL PROTEOME ANALYSIS: LABELING TECHNOLOGIES
FOR MASS SPECTROMETRY 105 JOSEF KELLERMANN 4.4.1 INTRODUCTION 105 4.4.2
ISOTOPIC LABELING OF PEPTIDES AND/OR PROTEINS 107 4.4.2.1 STABLE ISOTOPE
LABELING OF PROTEINS IN CELL CULTURE 107 4.4.2.2 CHEMICAL ISOTOPIC
LABELING OF PEPTIDES OR PROTEINS 108 4.4.2.3 SPIKING OF LABELED PEPTIDES
111 4.4.3 SUMMARY 111 4.4.4 PERSPECTIVES 112 4.4.5 RECIPE FOR BEGINNERS
112 REFERENCES 114 X CONTENTS 4.5 DETERMINING MEMBRANE PROTEIN
LOCALIZATION WITHIN SUBCEILULAR COMPARTMENTS USING STABLE ISOTOPE
TAGGING 118 KATHRYN S. LI HEY, TOM DUNKLEY, AND PAWE! SADOWSKI 4.5.1
INTRODUCTION 118 4.5.2 PREPARATION AND TREATMENT OF SAMPLES IN THE
EARLY-STAGE LOPIT PROTOCOL 120 4.5.2.1 PREPARATION AND FRACTIONATION OF
ORGANELLES 120 4.5.2.2 CARBONATE WASHING OF FRACTIONS TO LYSE
ORGANELLES, AND REMOVAL OF SOLUBLE AND PERIPHERAL PROTEINS 123 4.5.2.3
ITRAQ LABELING 124 4.5.3 APPLICATION OF LOPIT TO MAP THE ORGARIELLE
PROTEOME OF ARABIDOPSIS 125 4.5.4 SUMMARY 126 4.5.5 RECIPE FOR BEGINNERS
127 REFERENCES 127 5 ELECTROPHORESIS 129 5.1 SAMPLE PREPARATION FOR
TWO-DIMENSIONAL GEL ELECTROPHORESIS 129 WALTER WEISS AND ANGELIKA CORG
5.1.1 INTRODUCTION 129 5.1.2 GENERAL ASPECTS OF SAMPLE PREPARATION FOR
2-DGE 130 5.1.2.1 CELL DISRUPTION 130 5.1.2.2 SAMPLE CLEAN-UP 132
5.1.2.3 PROTEIN SOLUBILIZATION 135 5.1.3 APPLICATION SAMPLES 137 5.1.3.1
MAMMALIAN TISSUES 138 5.1.3.2 MICROBIAL CELL CULTURES 138 5.1.3.3 PLANT
CELLS 138 5.1.4 SUMMARY 139 5.1.5 PERSPECTIVE 140 5.1.6 RECIPES FOR
BEGINNERS 141 REFERENCES 142 5.2 SAMPLE PREPARATION FOR NATIVE
ELECTROPHORESIS 144 ILKA WITTIG AND HERMANN SCHAGGER 5.2.1 INTRODUCTION
144 5.2.2 SAMPLE PREPARATION: GENERAL CONSIDERATIONS 146 5.2.2.1 CHOICE
OF DETERGENT AND DETERGENT/PROTEIN RATIO 146 5.2.2.2 CHOICE OF IONIC
STRENGTH AND PH FOR SAMPLE SOLUBILIZATION 147 5.2.2.3 STORAGE OF
BIOLOGICAL MEMBRANES 148 5.2.2.4 EFFECTS OF ADDING COOMASSIE DYE TO
SAMPLE AND/OR CATHODE BUFFER FOR BNE 149 5.2.3 APPLICATIONS 150 5.2.3.1
SOLUBILIZATION OF BACTERIAL MEMBRANES, YEAST AND MAMMALIAN MITOCHONDRIA
250 CONTENTS \ X! 5.2.3.2 HOMOGENIZATION AND SOLUBIIIZATION OF MAMMALIAN
CELLS AND TISSUES 150 5.2.3.3 RECIPE FOR BEGINNERS: MASS CALIBRATION
LADDER FOR BNE 151 5.2.4 SUMMARY AND PERSPECTIVES 151 REFERENCES 152 5.3
SAMPLE PREPARATION FOR LC-MS/MS USING FREE-FLOW ELECTROPHORESIS 155
MIKKE! NISSUM, AFICMEH ABDOLZADE-BAVIL, SAB'ME KUHFUSS, ROBERT
WILDGRUBER, GERHARD WEBER, AND CHRISTOPH ECKERSKOM 5.3.1 INTRODUCTION
155 5.3.2 THE PROBLEMS OF SAMPLE PREPARATION: THE PROS AND CONS 157
5.3.2.1 SEPARATION 157 5.3.2.2 EXTRACTION 158 5.3.2.3 MEDIA COMPOSITION
158 5.3.3 APPLICATION EXAMPLE 159 5.3.3.1 REAGENTS 159 5.3.3.2 SAMPLE
PREPARATION FOR FFE 160 5.3.3.3 FFE SEPARATION OF PEPTIDES 160 5.3.3.4
RPLC-MS/MS ANALYSIS 161 5.3.3.5 DATA PROCESSING 161 5.3.4 SUMMARY 161
5.3.5 PERSPECTIVE 165 5.3.6 RECIPE FOR BEGINNERS 166 5.3.6.1 FFE SET-UP
PROCEDURE 166 5.3.6.2 PRE-EXPERIMENTAL QUALITY CONTROL (QC) 167 5.3.6.3
EXPERIMENT 168 REFERENCES 168 5.4 SAMPLE PREPARATION FOR CAPILLARY
ELECTROPHORESIS 171 ROSS BURN AND DAVID PERRETT 5.4.1 INTRODUCTION 171
5.4.2 SAMPLE PREPARATION 173 5.4.2.1 SAMPLE COLLECTION AND STORAGE 174
5.4.2.2 SAMPLE PREPARATION FOR CE 174 5.4.2.3 SAMPLE CONCENTRATION 175
5.4.2.4 OFF-LINE PRECONCENTRATION 275 5.4.2.5 ON-LINE PRECONCENTRATION
175 5.4.2.6 DESALTING 176 5.4.2.7 ANALYTE MODIFICATION 176 5.4.3
BACKGROUND ELECTROLYTE 277 5.4.4 CAPILLARY PREPARATION 178 5.4.4.1
CAPILLARY DIMENSIONS 178 5.4.4.2 CAPILLARY CONDITIONING 178 5.4.4.3
CAPILLARY COATING 179 5.4.5 SUMMARY 179 XII CONTENTS 5.4.6 PERSPECTIVE
179 5.4.7 RECIPE FOR BEGINNERS 180 5.4.7.1 METHOD 1: ANALYSIS OF HUMAN
SERUM/PLASMA BY C2E 180 5.4.7.2 METHOD 2: ANALYSIS OF TRYPTIC DIGESTS BY
CZE 282 5.4.7.3 METHOD 3: ANALYSIS OF PROTEOMES BY CIEF 183 REFERENCES
185 6 OPTICAL METHODS 187 6.1 HIGH-THROUGHPUT PROTEOMICS: SPINNING DISC
INTERFEROMETRY (SDI) 187 PATRICIO ESPINOZA VALLEJOS, GREG LAWRENCE,
DAVID NOLTE, FRED REGNIER, AND JOERG SCHREIBER 6.1.1 PROTEOMICS AS A
TOOL FOR HEALTH ASSESSMENT 287 6.1.2 TRANSLATIONAL PROTEOMICS 188 6.1.3
THE PRINCIPLES OF SPINNING DISC INTERFEROMETRY 189 6.1.3.1 THE SPINNING
DISC 289 6.1.3.2 WHY SPIN? 191 6.1.3.3 IN-LINE QUADRATURE 292 6.1.3.4
SCALING MASS SENSITIVITY 194 6.1.4 THE SPINNING DISC AS A
HIGH-THROUGHPUT IMMUNOLOGICAL ASSAY PLATFORM 2 96 6.1.4.1 IMMUNOLOGICAL
ASSAYS USING A DISC ARRAY FORMAT 297 6.1.4.2 ASSAY FORMATS 298 6.1.4.3
ASSAY PROTOCOLS 299 6.1.5 TYPES OF ASSAY THAT FIT THE SPINNING DISC 200
6.1.5.1 ASSAY STRUCTURE 200 6.1.5.2 ASSAY DEVELOPMENT KIT (ADK) 202
6.1.6 ASSAY AND SAMPLE PROCESSING 202 6.1.6.1 HIGH-THROUGHPUT SYSTEM 201
6.1.6.2 THE ADK 203 6.1.7 CONCLUSIONS 205 REFERENCES 206 6.2 OPTICAL
PROTEOMICS ON CELL ARRAYS 208 ANDREAS QROD AND PHILIPPE BASTIAENS
INTRODUCTION 208 A DESCRIPTION OF THE PROBLEM WITH REGARDS TO SAMPLE
PREPARATION 22 2 GENERAL REMARKS 22 2 CELL LINE SELECTION 222 SAMPLE
PREPARATION 222 CHOICE OF TRANSFECTION REAGENT 222 NUCLEIC ACID
PREPARATION 223 SAMPLE SCALE: HOW MANY DUPLICATES ARE REQUIRED? 223
CHOICE OF MICROARRAYER/MICROSPOTTING SYSTEM (SPOTTER) 223 LAYOUT DESIGN
(SPOTTING PATTERN) 224 6.2. 6.2. .1 .2 6.2.2.1 6.2.2.2 6.2. 6.2. 6.2.
6.2. 6.2. 6.2. .2.3 .2.4 .2.5 .2.6 .2.7 .2.8 CONTENTS XII! 6.2.3 SUMMARY
215 6.2.4 PERSPECTIVES 235 6.2.5 SAMPLE PREPARATION: SHORT PROTOCOL 215
6.2.5.1 RECOMMENDED EQUIPMENT AND CONSUMABLES 215 6.2.5.2 PREPARATION OF
THE SOURCE PLATE 216 6.2.5.3 SPOTTING 217 6.2.5.4 CELL CULTURE AND
EXPERIMENT 217 REFERENCES 218 6.3 SAMPLE PREPARATION BY LASER
MICRODISSECTION AND CATAPULTING FOR PROTEOME ANALYSIS 219 KARIN SCHUTZE,
ANDREA BUCHSTALLER, YILMAZ NIYAZ, CHRISTIAN MELLE, CUNTHER ERNST,
KERSTIN DAVID, THORSTEN SCHLOMM, AND FERDINAND VON EGGELING 6.3.1
INTRODUCTION: LASER MICRODISSECTION AND FUNCTIONAL PROTEOMIC RESEARCH
219 6.3.2 THE RELEVANCE OF PURE STARTING MATERIAL FOR PROTEOMICS 219
6.3.3 EXAMPLES OF COMBINED LMPC AND PROTEOMIC ANALYSES 220 6.3.3.1 LMPC
AND PREECLAMPSIA 220 6.3.3.2 LMPC AND RENAL CELL CARCINOMA 221 6.3.3.3
LMPC AND HEPATOCELLULAR CARCINOMA 221 6.3.3.4 LMPC AND BRAIN DISORDERS
221 6.3.3.5 LMPC AND PLANT BIOLOGY 221 6.3.4 LMPC ADAPTED FOR PROTEOMIC
APPLICATIONS 222 6.3.5 LMPC COMBINED WITH SELDI-TOF MS: A PROMISING
APPROACH FOR PATIENT-SPECIFIC ANALYSES 224 6.3.6 CORRELATION OF GENE AND
PROTEIN EXPRESSION: THE BEST DATA CAPTURE FOR COMPREHENSIVE DIAGNOSIS
228 6.3.7 RECIPE FOR BEGINNERS 228 6.3.7.1 PATIENTS AND SPECIMENS 228
6.3.7.2 LASER MICRODISSECTION OF TISSUE SECTIONS 230 6.3.7.3 PROTEINCHIP
ARRAY PREPARATION AND ANALYSIS 230 6.3.8 SUMMARY AND OUTLOOK 231
REFERENCES 232 6.4 SAMPLE PREPARATION FOR FLOW CYTOMETRY 234 DEREK C. DA
VIES 6.4.1 I NTR ODUCTIO N 234 6.4.2 SAMPLE PREPARATION FOR FLOW
CYTOMETRY 236 6.4.2.1 PREPARATION FROM CELLS IN SUSPENSION 236 6.4.2.2
PREPARATION FROM ADHERENT CELLS 237 6.4.2.3 PREPARATION FROM SOLID
TISSUE 237 6.4.2.4 GENERAL CONSIDERATIONS 237 6.4.3 IDENTIFICATION OF
RELEVANT CELLS 238 6.4.4 CELL SORTING 238 6.4.4.1 CELLS AND SAMPLES 238
6.4.4.2 CYTOMETER CONSIDERATIONS 239 XIV CONTENTS 6.4.5 APPLICATION
EXAMPLE 240 6.4.6 SUMMARY 242 6.4.7 PERSPECTIVES 242 6.4.8 RECIPES FOR
BEGINNERS 242 6.4.8.1 CULTURED SUSPENSION CELLS 242 6.4.8.2 ADHERENT
CELLS 242 6.4.8.3 SOLID TISSUE 243 REFERENCES 243 7 CHROMATOGRAPHY 245
7.1 SAMPLE PREPARATION FOR HPLC-BASED PROTEOME ANALYSIS 245 EGIDIJUS
MACHTEJEVAS AND KLAUS K. LINGER 7.1.1 INTRODUCTION 245 7.1.2 PROBLEMS
RELATED TO DIRECT SAMPLE INJECTION IN HPLC 246 7.1.3 TRIAL AND ERROR
SELECTION OF THE SAMPLE PREPARATION METHOD 247 7.1.4 CLASSICAL
APPROACHES 249 7.1.5 SPECIFIC APPROACHES APPLIED TO SAMPLE CLEAN-UP IN
PROTEOMICS 250 7.1.5.1 MINIATURIZED EXTRACTION TECHNIQUES 250 7.1.5.2
MOST ABUNDANT COMPONENT DEPLETION 250 7.1.5.3 AFFINITY-ENRICHMENT
APPROACHES 251 7.1.6 ON-LINE SAMPLE CLEAN-UP APPROACHES 252 I.X.I
RESTRICTED ACCESS TECHNOLOGY 254 7.1.8 APPLICATION EXAMPLE: THE CASE
STUDY 259 7.1.9 CONCLUSION AND PERSPECTIVES 260 REFERENCES 262 7.2
SAMPLE PREPARATION FOR TWO-DIMENSIONAL PHOSPHOPEPTIDE MAPPING AND
PHOSPHOAMINO ACID ANALYSIS 265 ANAMARIJA KRULJAC-LETUNIC AND ANDREE
BLAUKAT 7.2.1 INTRODUCTION 265 7.2.2 IMPORTANT ASPECTS IN SAMPLE
PREPARATION PROCEDURES 265 7.2.3 APPLICATION EXAMPLE 267 7.2.4 SUMMARY
267 7.2.5 PERSPECTIVE 269 7.2.6 RECIPE FOR BEGINNERS 269 7.2.6.1 2-D
PHOSPHOPEPTIDE MAPPING PROCEDURE 269 7.2.6.2 PHOSPHOAMINO ACID ANALYSIS
PROCEDURE 271 REFERENCES 271 8 STRUCTURAL PROTEOMICS 273 8.1 EXPLORING
PROTEIN-LIGAND INTERACTIONS BY SOLUTION NMR 273 RUDOLF HARTMANN, THOMAS
STANGLER, BERND W.KONIG, AND DIETER WILLBOLD 8.1.1 INTRODUCTION 273
8.1.2 LOCALIZATION OF INTERACTION SITES BY CHEMICAL SHIFT PERTURBATION
(CSP) MAPPING 274 CONTENTS XV 8.1.3 SATURATION TRANSFER DIFFERENCE
SPECTROSCOPY 276 8.1.4 LIGAND SCREENING BY NMR 278 REFERENCES 2,79 8.2
SAMPLE PREPARATION FOR CRYSTALLOGRAPHY 281 DJORDJE MUSIL INTRODUCTION
281 USE OF RECOMBINANT PROTEINS IN CRYSTALLIZATION 282 PROTEIN
SOLUBILITY AND CRYSTALLIZATION 284 PROTEIN CRYSTALLIZATION 286 PRACTICAL
EXAMPLES 291 REFERENCES 292 INTERACTION ANALYSIS 295 SAMPLE PREPARATION
FOR PROTEIN COMPLEX ANALYSIS BY THE TANDEM AFFINITY PURIFICATION (TAP)
METHOD 295 BERTRAND SERAPHIM AND ANDRZEJ DZIEMBOWSKI INTRODUCTION 295
THE PROBLEM WITH REGARDS TO SAMPLE PREPARATION: THE PROS AND THE CONS
296 APPLICATION EXAMPLE 300 SUMMARY 301 PERSPECTIVE 301 RECIPE FOR
BEGINNERS 301 REFERENCES 302 9.2 EXPLORING MEMBRANE PROTEOMES 303
FILIPPA STENBERG AND DANIEL O. DALEY 9.2.1 INTRODUCTION 303 9.2.2
DENNING MEMBRANE PROTEOMES 303 9.2.3 SEPARATION OF MEMBRANE PROTEOMES
304 9.2 A EXPERIMENTAL IDENTIFICATION OF MEMBRANE PROTEINS 307 9.2.5
MAPPING MEMBRANE INTERACTOMES 307 9.2.6 STRUCTURAL ANALYSIS OF MEMBRANE
PROTEOMES 308 9.2.7 SUMMARY AND PERSPECTIVE 309 9.2.8 RECIPE FOR
BEGINNERS 311 9.2.8.1 SAMPLE PREPARATION 311 9.2.8.2 BN-PAGE 311 9.2.8.3
SDS-PAGE 312 REFERENCES 312 10 POST-TRANSLATIONAL MODIFICATIONS 317 10.1
SAMPLE PREPARATION FOR PHOSPHOPROTEOME ANALYSIS 317 RENE P. ZAHEDI AND
ALBERT SICKMANN 10.1.1 INTRODUCTION 317 10.1.2 GENERAL SAMPLE
PREPARATION 317 8.2 .1 8.2.2 8.2 8.2 8.2 9 9.1 9.1 9.1 9.1 9.1 9.1 9.1
.3 .4 .5 .1 .2 .3 .4 .5 .6 XVI CONTENTS 10.1.3 REDUCTION OF SAMPLE
COMPLEXITY 318 10.13.1 GEL ELECTROPHORESIS 318 10.1.3.2 ISOELECTRIC
FOCUSING 318 10.1.4 METHODS FOR PHOSPHOPEPTIDE/PROTEIN ENRICHMENT 319
10.1.4.1 IMMUNOPRECIPITATION 319 10.1.4.2 IMMOBILIZED METAL ION AFFINITY
CHROMATOGRAPHY (IMAC) 319 10.1.4.3 METAL OXIDES 320 10.1.4.4
CATION-EXCHANGE CHROMATOGRAPHY 321 10.1.4.5 DERIVATIZATION APPROACHES
322 10.1.5 SUMMARY 323 10.1.6 PERSPECTIVE 324 10.1.7 RECIPE FOR
BEGINNERS: IMAC 324 REFERENCES 325 10.2 SAMPLE PREPARATION FOR ANALYSIS
OF POST-TRANSLATIONAL MODIFICATIONS: GLYCOSYLATION 328 DAVID S. SELBY,
MARTIN R. LARSEN, MIRENJ. OMAETXEHARRIA, AND PETER ROEPSTORJF 10.2.1
INTRODUCTION 328 10.2.2 ADVANTAGES AND DISADVANTAGES OF DIFFERENT SAMPLE
PREPARATION METHODS 331 10.2.3 EXAMPLE APPLICATIONS OF ENRICHMENT
METHODS 334 10.2.3.1 ZIC-HILIC MICROCOLUMNS FOR PREPARATION OF N-LINKED
GLYCAN-CONTAINING SAMPLES 334 10.2.3.2 TITANIUM DIOXIDE MICROCOLUMNS FOR
ENRICHMENT OF SIALIC ACID-CONTAINING GLYCOPEPTIDES AND
GLYCOSYLPHOSPHATIDYLINOSITOL LIPID-ANCHORED PEPTIDES 336 10.2.4 SUMMARY
337 10.2.5 PERSPECTIVE 338 10.2.6 RECIPE FOR BEGINNERS: ENRICHMENT OF
GLYCOPEPTIDES WITH A HILIC MICROCOLUMN 338 10.2.6.1 MATERIALS 338
10.2.6.2 PROCEDURE: PURIFICATION OF GLYCOPEPTIDES 339 10.2.6.3
PROCEDURE: DEGLYCOSYLATION OF N-LINKED GLYCOPEPTIDES 339 REFERENCES 340
11 SPECIES-DEPENDENT PROTEOMICS 343 11.1 SAMPLE PREPARATION AND DATA
PROCESSING IN PLANT PROTEOMICS 343 KATJA BAERENFALLER, WILHELM GRUISSEM,
AND SACHA BAGINSKY 11.1.1 INTRODUCTION 343 1.1.1.2 PLANT-SPECIFIC
CONSIDERATIONS IN PROTEOMICS 344 11.1.2.1 CELL WALLS 344 11.1.2.2
PLASTIDS 344 11.1.2.3 PROTEIN EXTRACTION FROM PLANT TISSUE 345 11.1.2.4
EXTRACTION FROM RECALCITRANT AND RESISTANT TISSUE 345 XVI! 11.1.2.5
DYNAMIC RANGE LIMITATIONS 346 11.1.2.6 PROTEORNICS IN AS-YEL UNSEQUENCED
ORGANISMS 346 11.1.3 SAMPLE PREPARATION PROTOCOLS 347 11.13.1 CEIL WAIL
PROTEIN EXTRACTION 348 11.13.2 PLASTIC! ISOLATION 349 11.1.3.3 PROTEIN
EXTRACTION WITH TCA/ ACETONE 350 11.1.3.4 PHENOL EXTRACTION 35 1
11.1.3.5 SERIAL EXTRACTION 351 11.1.3.6 EXTRACTION FROM RECALCITRANT AND
RESISTANT TISSUE 352 11.1.3.7 EXTRACTION AND FRACTIONATION WITH
POLYETHYLENE GLYCOL (PEG) 353 11.1.3.8 STAGES FOLLOWING PROTEIN
EXTRACTION 353 11.1.4 MS/MS DATA PROCESSING FOR UNSEQUENCED ORGANISMS
354 11.1.5 CONCLUDING REMARKS 355 REFERENCES 356 11.2 SAMPLE PREPARATION
FOR MUDPIT WITH BACTERIAL PROTEIN SAMPLES 358 ANSGAR POETSCH AND DIRK
WOLTERS 11.2.1 INTRODUCTION 358 11.2.2 THE MUDPIT TECHNOLOGY 359 11.2.3
MEMBRANE PROTEINS AND MUDPIT 361 11.2.4 QUANTITATIVE MUDPIT 363 11.2.5
LIMITATIONS OF MUDPIT 364 11.2.6 PITFALLS OF MUDPIT 365 11.2.7 SUMMARY
365 11.2.8 PERSPECTIVE 365 11.2.9 RECIPE FOR BEGINNERS: MUDPIT: SOLUBLE
AND MEMBRANE PROTEINS 366 REFERENCES 368 11.3 SAMPLE PREPARATION FOR THE
CELL-WALL PROTEOME ANALYSIS OF YEAST AND FUNGI 371 KAI SOHN, EKKEHARD
HITLER, AND STEFFEN RUPP 11.3.1 INTRODUCTION 371 113.2 DESCRIPTION OF
THE PROBLEM WITH REGARDS TO SAMPLE PREPARATION 372 11.3.3 APPLICATION
EXAMPLE 373 11.3.4 SUMMARY 375 11.3.5 PERSPECTIVE 376 11.3.6 RECIPE FOR
BEGINNERS 376 113.6.1 CULTURES 376 113.6.2 PREPARATION OF SOLUBLE
CELL-SURFACE PROTEINS 376 113.6.3 PREPARATION OF PEPTIDES FROM
COVALENTLY LINKED CELL-WALL PROTEINS 377 REFERENCES 378 12 THE HUMAN
PROTEOSOME 379 12.1 CLINICAL PROTEOMICS: SAMPLE PREPARATION AND
STANDARDIZATION 379 GERD SCHMITZ AND CARSTEN GNEWUCH 12.1.1 INTRODUCTION
379 XVIII CONTENTS 12.1.2 THE PREANALYTICAL PHASE: SAMPLE PREPARATION,
STANDARDIZATION, AND QUALITY MANAGEMENT 380 12.1.2.1 STANDARDIZATION OF
THE (PRE)-ANALYTICAL PROCESS 381 12.1.3 PROTEOMICS IN BODY FLUIDS 382
12.1.3.1 TECHNIQUES FOR PROTEOMIC ANALYSIS 382 12.1.3.2 APPLICATIONS 383
12.1.3.3 PREPARATION OF CLINICAL SAMPLES FOR FLUIDIC PROTEOMICS 386
12.1.4 CELLULAR PROTEOMICS (CYTOMICS) 389 12.1.4.1 SAMPLE PREPARATION
AND STANDARDIZATION FOR CLINICAL CYTOMICS 389 12.1.4.2 TISSUE ARRAYS 390
12.1.4.3 BEAD-BASED IMMUNOASSAYS FOR PROTEIN ANALYSIS 391 12.1.4.4
PREPARATIVE METHODS 391 12.1.4.5 CLINICAL APPLICATIONS IN CYTOMICS 399
12.1.5 CONCLUSION 404 REFERENCES 405 12.2 STERN CELL PROTEOMICS 412
REGINA EBERT, GABRIELE MOLLER, JERZY ADAMSKI, AND FRANZ JAKOB 12.2.1
INTRODUCTION 412 12.2.2 STEM CELL NICHES 413 12.2.3 WHY STUDY PROTEOMES
IN STEM CELLS? 413 12.2.4 TECHNICAL CHALLENGES AND PROBLEMS 414 12.2.4.1
STEM CELL PREPARATION 414 12.2.4.2 CULTIVATION 415 12.2.4.3 TREATMENT
415 12.2.4.4 WHOLE-CELL PROTEOME 415 12.2.4.5 SECRETORY PROTEOME 425
12.2.5 RECIPES FOR BEGINNERS 417 12.2.5.1 WHOLE-CELL LYSATE 417 12.2.5.2
SECRETORY PROTEOME PROCEDURE 418 12.2.5.3 LABELING WITH 35 S 418
12.2.5.4 ETHANOL PRECIPITATION 419 12.2.5.5 TCA PRECIPITATION 4 1 9
REFERENCES 419 13 BIOINFORMATICS 423 13.1 BIOINFORMATICS SUPPORT FOR
MASS SPECTROMETRIC QUALITY CONTROL 423 KNUT REINERT, TIM CONRAD, AND
OLIVER KOHLBACHER 13.1.1 INTRODUCTION 423 13.1.2 PROBLEM DESCRIPTION 423
13.1.2.1 SIGNAL PROCESSING PITFALLS 424 13.1.2.2 MAP QUALITY CONTROL 425
13.1.2.3 STATISTICAL VALIDATION RESULTS 425 13.1.3 QUALITY ASSESSMENT
FOR ONE-DIMENSIONAL (1-D) MS DATA 426 13.1.3.1 FILTER 427 CONTENTS I XIX
13.1.4 APPLICATION EXAMPLE; ABSOLUTE QUANTIFICATION OF AN UNKNOWN
PEPTIDE CONTENT 428 13.1.5 SUMMARY 429 13.1.6 PERSPECTIVE 430 13.1.7
RECIPE FOR BEGINNERS 430 13.1.7.1 ACQUIRING THE RA W DATA 430 13.1.7.2
PREPROCESSING THE DATA 431 13.1.7.3 ANALYZING THE PREPROCESSED DATA 431
REFERENCES 431 13.2 USE OF PHYSICO-CHEMICAL PROPERTIES IN PEPTIDE AND
PROTEIN IDENTIFICATION 433 ANASTASIA K. YOCUM, PETERJ. ULINTZ, AND
PHILIP C. ANDREWS 13.2.1 INTRODUCTION 433 13.2.2 ISOELECTRIC POINT 434
13.2.3 ION-EXCHANGE CHROMATOGRAPHY 436 13.2.4 REVERSED-PHASE
CHROMATOGRAPHY 438 13.2.5 MASS ACCURACY 442 13.2.6 SUMMARY 443
REFERENCES 444 INDEX 449 |
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| illustrated | Illustrated |
| index_date | 2024-07-02T21:06:50Z |
| indexdate | 2024-07-20T09:42:40Z |
| institution | BVB |
| isbn | 9783527317967 |
| language | English |
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| physical | XXXII, 453 S. Ill., graph. Darst. 24 cm |
| publishDate | 2008 |
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| publisher | Wiley-VCH-Verl. |
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| spelling | Proteomics sample preparation ed. by Jörg von Hagen Weinheim Wiley-VCH-Verl. 2008 XXXII, 453 S. Ill., graph. Darst. 24 cm txt rdacontent n rdamedia nc rdacarrier Literaturangaben Analytic Sample Preparation Methods Proteins Analysis Proteins analysis Proteomics Proteomics methods Probenvorbereitung (DE-588)4588977-6 gnd rswk-swf Proteomanalyse (DE-588)4596545-6 gnd rswk-swf Proteomanalyse (DE-588)4596545-6 s Probenvorbereitung (DE-588)4588977-6 s DE-604 Hagen, Jörg von 1969- Sonstige (DE-588)129386715 oth text/html http://deposit.dnb.de/cgi-bin/dokserv?id=2945662&prov=M&dok_var=1&dok_ext=htm Inhaltstext SWBplus Fremddatenuebernahme application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016539017&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Proteomics sample preparation Analytic Sample Preparation Methods Proteins Analysis Proteins analysis Proteomics Proteomics methods Probenvorbereitung (DE-588)4588977-6 gnd Proteomanalyse (DE-588)4596545-6 gnd |
| subject_GND | (DE-588)4588977-6 (DE-588)4596545-6 |
| title | Proteomics sample preparation |
| title_auth | Proteomics sample preparation |
| title_exact_search | Proteomics sample preparation |
| title_exact_search_txtP | Proteomics sample preparation |
| title_full | Proteomics sample preparation ed. by Jörg von Hagen |
| title_fullStr | Proteomics sample preparation ed. by Jörg von Hagen |
| title_full_unstemmed | Proteomics sample preparation ed. by Jörg von Hagen |
| title_short | Proteomics sample preparation |
| title_sort | proteomics sample preparation |
| topic | Analytic Sample Preparation Methods Proteins Analysis Proteins analysis Proteomics Proteomics methods Probenvorbereitung (DE-588)4588977-6 gnd Proteomanalyse (DE-588)4596545-6 gnd |
| topic_facet | Analytic Sample Preparation Methods Proteins Analysis Proteins analysis Proteomics Proteomics methods Probenvorbereitung Proteomanalyse |
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