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1 online resource
  • Front Cover; Applications in High Resolution Mass Spectrometry; Applications in HighResolution Mass Spectrometry: Food Safety and Pesticide Residue Analysis; Copyright; Contents; List of Contributors; Preface; 1
  • 5
  • Advanced Sample Preparation Techniques for Pesticide Residues Determination by HRMS Analysis
online resource (xiv, 298 pages) : illustrations (some color)
Medical Library (Lane)
1 online resource.
  • Overview, Pitfalls, Hardware-Requirements. State of the Art in the LC/MS / O Schmitz
  • Technical Aspects and Pitfalls of LC/MS Hyphenation / MM Martin
  • Aspects of the Development of Methods in LC/MS Coupling / T Teutenberg, T Hetzel, C Portner, S Wiese, C Eyser, J Tuerk
  • Tips, Examples, Trends. LC/MS for Everybody/for Everything? - LC/MS Tips / F Mandel
  • User Reports. LC Coupled to MS - a User Report / A Muller, A Hofmann
  • Problem Solving with HPLC/MS - a Practical View from Practitioners / E Fleischer
  • LC/MS from the Perspective of a Maintenance Engineer / O Müller
  • Vendor's Reports. LC/MS - the Past, Present, and Future / TL Sheehan, F Mandel
  • Vendor's Report - SCIEX / D Schleuder
  • Manufacturer Report - Thermo Fisher Scientific / MM Martin.
1 online resource (p. 1-14 ): digital, PDF file.
Clostridium thermocellum is capable of solubilizing and converting lignocellulosic biomass into ethanol. Though much of the work-to-date has centered on characterizing the organism s metabolism during growth on model cellulosic substrates, such as cellobiose, Avicel, or filter paper, it is vitally important to understand it metabolizes more complex, lignocellulosic substrates to identify relevant industrial bottlenecks that could undermine efficient biofuel production. To this end, we have examined a time course progression of C. thermocellum grown on switchgrass to assess the metabolic and protein changes that occur during the conversion of plant biomass to ethanol. The most striking feature of the metabolome was the observed accumulation of long-chain, branched fatty acids over time, implying an adaptive restructuring of C. thermocellum s cellular membrane as the culture progresses. This is likely a response to the gradual build-up of lignocellulose-derived inhibitory compounds detected as the organism deconstructs the switchgrass to access the embedded cellulose and includes 4-hydroxybenzoic acid, vanillic acid, ferulic acid, p-coumaric acid and vanillin. Corroborating the metabolomics data, proteomic analysis revealed a corresponding time-dependent increase in enzymes involved in the interconversion of branched amino acids valine, leucine and isoleucine to iso- and anteiso-fatty acid precursors. Furthermore, the metabolic accumulation of hemicellulose-derived sugars and sugar-alcohols concomitant with increased abundance of enzymes involved in C5 sugar metabolism / the pentose phosphate pathway, indicate that C. thermocellum either shifts glycolytic intermediates to alternate pathways to modulate overall carbon flux or is simply a response to C5 sugar metabolite pools that build during lignocellulose deconstruction.
xiv, 393 pages : illustrations ; 29 cm.
  • Preface xi Abbreviations xiii 1 Introduction to LC-MS Technology 1 1.1 Introduction 2 1.2 Analyte Ionization: Ion Sources 3 1.2.1 Electron Ionization 3 1.2.2 Chemical Ionization 7 1.2.3 Atmospheric-Pressure Ionization 13 1.2.4 Electrospray Ionization 16 1.2.5 Atmospheric-Pressure Chemical Ionization and Photoionization 20 1.2.6 Other Ionization Techniques 26 1.3 Mass Spectrometer Building Blocks 28 1.3.1 Introduction 28 1.3.2 Quadrupole Mass Analyzer 32 1.3.3 Ion-Trap Mass Analyzer 33 1.3.4 Time-of-Flight Mass Analyzer 34 1.3.5 Orbitrap Mass Analyzer 35 1.3.6 Other Mass Analyzers 36 1.4 Tandem Mass Spectrometry 37 1.4.1 Introduction 37 1.4.2 Tandem Quadrupole Instruments 39 1.4.3 Ion-Trap Instruments 40 1.4.4 Quadrupole-Linear Ion-Trap Hybrid Instruments 41 1.4.5 Quadrupole-Time-of-Flight Hybrid Instruments 41 1.4.6 Orbitrap Hybrid Instruments for MS-MS and MSn 41 1.4.7 Other Instruments for MS-MS and MSn 42 1.4.8 MS-MS and MSn in the Analysis of Drugs and Pesticides 43 1.5 Data Acquisition 43 1.5.1 Introduction 43 1.5.2 Selected-Ion and Selected-Reaction Monitoring 44 1.5.3 Structure-Specific Screening: Precursor-Ion and Neutral-Loss Analysis 44 1.5.4 Data-Dependent Acquisition 45 1.5.5 Data-Independent Acquisition 45 1.6 Selected Literature on Mass Spectrometry 45 2 Interpretation of Mass Spectra 55 2.1 Mass Spectrometry: A Nuclear Affair 55 2.2 Isomers, Isotones, Isobars, Isotopes 56 2.3 Masses in MS 58 2.4 Isotopes and Structure Elucidation 60 2.5 Nitrogen Rule, Ring Double-Bond Equivalent, and Hydrogen Rule 61 2.6 Resolving Power, Resolution, Accuracy 63 2.7 Calculating Elemental Composition from Accurate m/z 66 2.8 Protonated and Deprotonated Molecules and Adduct Ions 67 3 Fragmentation of Even-Electron Ions 71 3.1 Introduction 72 3.2 Analyte Ionization Revisited 73 3.3 Fragmentation of Odd-electron Ions 74 3.4 High-energy Collisions of Protonated Molecules 76 3.4.1 General Aspects 77 3.4.2 Selected Examples 79 3.5 Fragmentation of Protonated Molecules 81 3.5.1 Singly-Charged Peptides 82 3.5.2 Protonated Small Molecules: Complementary Fragment Ions 83 3.5.3 Fragmentation of Peptides Revisited 86 3.5.4 Direct-Cleavage Reactions 89 3.5.5 Consecutive Small-Molecule Losses 89 3.5.6 Other Fragmentation Reactions 89 3.5.7 Loss of Radicals from Even-Electron Ions 91 3.5.8 Skeletal Rearrangements in Protonated Molecules 92 3.6 Characteristic Positive-ion Fragmentation of Functional Groups 94 3.6.1 Cleavages of C-C Bonds 94 3.6.2 Alcohols and Ethers 95 3.6.3 Aldehydes and Ketones 96 3.6.4 Carboxylic Acids and Esters 96 3.6.5 Amines and Quaternary Ammonium Compounds 98 3.6.6 Amides, Sulfonyl Ureas, and Carbamates 99 3.6.7 Compounds containing Phosphorus or Sulfur 101 3.6.8 Miscellaneous Compound Classes 101 3.7 Fragmentation of Deprotonated Molecules 102 3.7.1 High-Energy CID with NICI-Generated Deprotonated Molecules 102 3.7.2 General Aspects 102 3.7.3 Alcohols and Ethers 102 3.7.4 Carboxylic Acid and Esters 103 3.7.5 Amines 104 3.7.6 Amides and Ureas 104 3.7.7 Sulfonamides and Related Sulfones 106 3.7.8 Halogenated Compounds 107 3.7.9 Miscellaneous Compound Classes 108 3.8 Fragmentation of Metal-ion Cationized Molecules 108 3.9 Generation of Odd-electron Ions in ESI-MS, APCI-MS, and APPI-MS 111 3.10 Useful Tables 112 4 Fragmentation of Drugs and Pesticides 129 4.1 Fragmentation of Drugs for Cardiovascular Diseases and Hypertension 134 4.1.1 -Blockers or -Adrenergic Antagonists 134 4.1.2 Dihydropyridine Calcium Antagonists 137 4.1.3 Angiotensin-Converting Enzyme Inhibitors 140 4.1.4 Diuretic Drugs 142 4.1.5 Angiotensin II Receptor Antagonists 148 4.1.6 Other Antihypertensive Compounds 149 4.1.7 Antiarrhythmic Agents 153 4.2 Fragmentation of Psychotropic or Psychoactive Drugs 158 4.2.1 Phenothiazines 158 4.2.2 Other Classes of Neuroleptic Drugs 161 4.2.3 Antidepressants 163 4.2.4 Benzodiazepines 167 4.2.5 Local Anesthetics 173 4.2.6 Barbiturates 173 4.2.7 Anticonvulsant Drugs 174 4.2.8 Other Psychotropic Drugs 175 4.3 Fragmentation of Analgesic, Antipyretic, and Anti-Inflammatory Drugs 179 4.3.1 Acetaminophen 179 4.3.2 Salicylic Acid Derivatives 179 4.3.3 Nonsteroidal Anti-Inflammatory Drugs 180 4.3.4 COX-2 Inhibitors 184 4.4 Fragmentation of Drugs Related to Digestion and the Gastrointestinal Tract 188 4.4.1 Antidiabetic Drugs 188 4.4.2 Antiulcer Drugs 191 4.4.3 Lipid-Lowering Agents 192 4.4.4 Anorexic Drugs 195 4.4.5 Antiemetic Drugs 196 4.5 Fragmentation of Other Classes of Drugs 199 4.5.1 -Adrenergic Receptor Agonists 199 4.5.2 Histamine Antagonists 199 4.5.3 Anticholinergic Agents 202 4.5.4 Drugs against Alzheimer's Disease: Acetylcholinesterase Inhibitors 204 4.5.5 Antiparkinsonian Drugs 208 4.5.6 Antineoplastic and Cytostatic Drugs 209 4.5.7 Immunosuppressive Drugs 214 4.5.8 X-ray Contrast Agents 216 4.5.9 Anticoagulants and Rodenticides 218 4.5.10 Conclusions 219 4.6 Fragmentation of Steroids 222 4.6.1 Introduction 222 4.6.2 Fragmentation of Steroids 223 4.6.3 Fragmentation in 3-Keto- 4-Steroids 224 4.6.4 Anabolic Steroids 225 4.6.5 Progestogens 227 4.6.6 Corticosteroids 228 4.6.7 Estrogens 234 4.6.8 Steroid Conjugates 236 4.7 Fragmentation of Drugs of Abuse 241 4.7.1 Introduction 241 4.7.2 Amphetamine and Related Compounds 241 4.7.3 Cannabinoids 248 4.7.4 Cocaine and Related Substances 250 4.7.5 Opiates 251 4.7.6 Miscellaneous Drugs of Abuse 252 4.7.7 Designer Drugs 255 4.8 Fragmentation of Antimicrobial Compounds 262 4.8.1 Sulfonamides 262 4.8.2 Chloramphenicol and Related Compounds 265 4.8.3 -Lactams 266 4.8.4 (Fluoro)quinolones 273 4.8.5 Aminoglycosides 277 4.8.6 Tetracyclines 279 4.8.7 Nitrofurans 279 4.8.8 Macrolides 281 4.8.9 Miscellaneous Antibiotics 282 4.9 Fragmentation of Antimycotic and Antifungal Compounds 289 4.9.1 Imidazolyl Antimycotic Compounds 289 4.9.2 Triazolyl Antifungal Compounds 290 4.9.3 Benzamidazole Fungicides 292 4.9.4 Other Classes of Fungicides 293 4.10 Fragmentation of Other Antibiotic Compounds 297 4.10.1 Anthelmintic Drugs 297 4.10.2 Antiprotozoal, Coccidiostatic, and Antimalarial Agents 299 4.10.3 Antiviral Drugs 304 4.10.4 Antiseptics and Disinfectants 309 4.11 Pesticides 315 4.11.1 Triazine Herbicides 315 4.11.2 Carbamates 317 4.11.3 Quaternary Ammonium Herbicides 322 4.11.4 Organophosphorus Pesticides 322 4.11.5 Urea Herbicides: Phenylureas, Benzoylphenylureas, and Others 329 4.11.6 Sulfonylurea Herbicides 334 4.11.7 Chlorinated Phenoxy Acid Herbicides 337 4.11.8 Phenolic Compounds 339 4.11.9 Miscellaneous Herbicides 339 5 Identification Strategies 351 5.1 Introduction 351 5.2 Confirmation of Identity in Following Organic Synthesis 352 5.3 Confirmation of Identity in Targeted Screening by SRM-based Strategies 353 5.3.1 Environmental Analysis 354 5.3.2 Food Safety Analysis 355 5.3.3 Sports Doping Analysis 355 5.3.4 General Unknown Screening in Toxicology 355 5.4 Confirmation of Identity by High-resolution Accurate-mass MS Strategies 356 5.4.1 Environmental and Food Safety Analysis 356 5.4.2 General Unknown Screening in Toxicology 357 5.4.3 Sports Doping Analysis 357 5.5 Library Searching Strategies in Systematic Toxicological Analysis 357 5.6 Dereplication and Identification of Natural Products and Endogenous Compounds 360 5.7 Identification of Structure-related Substances 361 5.7.1 Drug Metabolites 362 5.7.2 Impurities and Degradation Products 366 5.8 Identification of Known Unknowns and Real Unknowns 366 Compound Index 381 Subject Index.
  • (source: Nielsen Book Data)9781118500187 20170313
Provides comprehensive coverage of the interpretation of LC MS MS mass spectra of 1300 drugs and pesticides * Provides a general discussion on the fragmentation of even-electron ions (protonated and deprotonated molecules) in both positive-ion and negative-ion modes * This is the reference book for the interpretation of MS MS mass spectra of small organic molecules * Covers related therapeutic classes of compounds such as drugs for cardiovascular diseases, psychotropic compounds, drugs of abuse and designer drugs, antimicrobials, among many others * Covers general fragmentation rule as well as specific fragmentation pathways for many chemical functional groups * Gives an introduction to MS technology, mass spectral terminology, information contained in mass spectra, and to the identification strategies used for different types of unknowns.
(source: Nielsen Book Data)9781118500187 20170313
Science Library (Li and Ma)
1 online resource
  • List of Contributors xxi Preface xxix Part I MALDI-TOF Mass Spectrometry 1 1 A Paradigm Shift from Research to Front ]Line Microbial Diagnostics in MALDI ]TOF and LC ]MS/MS: A Laboratory s Vision and Relentless Resolve to Help Develop and Implement This New Technology amidst Formidable Obstacles 3 Haroun N. Shah and Saheer E. Gharbia 2 Criteria for Development of MALDI ]TOF Mass Spectral Database 39 Markus Kostrzewa and Thomas Maier 3 Applications of MALDI ]TOF Mass Spectrometry in Clinical Diagnostic Microbiology 55 Onya Opota, Guy Prod hom and Gilbert Greub 4 The Challenges of Identifying Mycobacterium to the Species Level using MALDI ]TOF MS 93 5 Transformation of Anaerobic Microbiology since the Arrival of MALDI ]TOF Mass Spectrometry 123 Elisabeth Nagy, Mariann Abrok, Edith Urban, A.C.M. Veloo, Arie Jan van Winkelhoff, Itaru Dekio, Saheer E. Gharbia and Haroun N. Shah 6 Differentiation of Closely Related Organisms using MALDI ]TOF MS 147 Mark A. Fisher 7 Identification of Species in Mixed Microbial Populations using MALDI ]TOF MS 167 Pierre Mahe, Maud Arsac, Nadine Perrot, Marie ]Helene Charles, Patrick Broyer, Jay Hyman, John Walsh, Sonia Chatellier, Victoria Girard, Alex van Belkum, and Jean ]Baptiste Veyrieras 8 Microbial DNA Analysis by MALDI ]TOF Mass Spectrometry 187 9 Impact of MALDI ]TOF MS in Clinical Mycology-- Progress and Barriers in Diagnostics 211 Cledir R. Santos, Elaine Francisco, Mariana Mazza, Ana Carolina B. Padovan, Arnaldo Colombo and Nelson Lima 10 Development and Application of MALDI ]TOF for Detection of Resistance Mechanisms 231 Stefan Zimmermann and Irene Burckhardt 11 Discrimination of Burkholderia Species, Brucella Biovars, Francisella tularensis and Other Taxa at the Subspecies Level by MALDI ]TOF Mass Spectrometry 249 Axel Karger 12 MALDI ]TOF ]MS Based on Ribosomal Protein Coding in S10 ]spc ]alpha Operons for Proteotyping 269 Hiroto Tamura Part II Tandem MS/MS-Based Approaches to Microbial Characterization 311 13 Tandem Mass Spectrometry Analysis as an Approach to Delineate Genetically Related Taxa 313 Raju V. Misra, Tom Gaulton, Nadia Ahmod, Min Fang, Martin Hornshaw, Jenny Ho, Saheer E. Gharbia and Haroun N. Shah 14 Mapping of the Proteogenome of Clostridium difficile Isolates of Varying Virulence 379 Caroline H. Chilton, Saheer E. Gharbia, Raju V. Misra, Min Fang, Ian R. Poxton, Peter S. Borriello and Haroun N. Shah 15 Determination of Antimicrobial Resistance using Tandem Mass Spectrometry 399 Ajit J. Shah, Vlad Serafim, Zhen Xu, Hermine Mkrtchyan and Haroun N. Shah 16 Proteotyping: Tandem Mass Spectrometry Shotgun Proteomic Characterization and Typing of Pathogenic Microorganisms 419 Roger Karlsson, Lucia Gonzales ]Siles, Fredrik Boulund, Asa Lindgren, Liselott Svensson ]Stadler, Anders Karlsson, Erik Kristiansson and Edward R.B. Moore 17 Proteogenomics of Pseudomonas aeruginosa in Cystic Fibrosis Infections 451 Liang Yang and Song Lin Chua 18 Top ]Down Proteomics in the Study of Microbial Pathogenicity 493 Joseph Gault, Egor Vorontsov, Mathieu Dupre, Valeria Calvaresi, Magalie Duchateau, Diogo B. Lima, Christian Malosse and Julia Chamot ]Rooke 19 Tandem Mass Spectrometry in Resolving Complex Gut Microbiota Functions 505 Carolin Kolmeder, Kaarina Lahteenmaki, Pirjo Wacklin, Annika Kotovuori, Ilja Ritamo, Jaana Matto, Willem M. de Vos, and Leena Valmu 20 Proteogenomics of Non ]model Microorganisms 529 Jean Armengaud 21A Analysis of MALDI ]TOF MS Spectra using the BioNumerics Software 539 Katleen Vranckx, Katrien De Bruyne and Bruno Pot 21B Subtyping of Staphylococcus spp. Based upon MALDI ]TOF MS Data Analysis 563 Zhen Xu, Ali Olkun, Katleen Vranckx, Hermine V. Mkrtchyan, Ajit J. Shah, Bruno Pot, Ronald R. Cutler and Haroun N. Shah 21C Elucidating the Intra ]Species Proteotypes of Pseudomonas aeruginosa from Cystic Fibrosis 579 Ali Olkun, Ajit J. Shah and Haroun N. Shah References 588 Index 593.
  • (source: Nielsen Book Data)9781118960257 20170424
This book highlights the triumph of MALDI-TOF mass spectrometry over the past decade and provides insight into new and expanding technologies through a comprehensive range of short chapters that enable the reader to gauge their current status and how they may progress over the next decade. This book serves as a platform to consolidate current strengths of the technology and highlight new frontiers in tandem MS/MS that are likely to eventually supersede MALDI-TOF MS. Chapters discuss: Challenges of Identifying Mycobacterium to the Species level Identification of Bacteroides and Other Clinically Relevant Anaerobes Identification of Species in Mixed Microbial Populations Detection of Resistance Mechanisms Proteomics as a biomarker discovery and validation platform Determination of Antimicrobial Resistance using Tandem Mass Spectrometry.
(source: Nielsen Book Data)9781118960257 20170424
1 online resource.
  • List of Contributors xvii Introduction xxi List of Abbreviations xxiii 1 Mass Spectrometry Techniques for In Vivo Stable Isotope Approaches 1 Jean-Philippe Godin and Henk Schierbeek 1.1 Introduction 1 1.2 Nomenclature for Light-Stable Isotope Changes 3 1.3 Mass Spectrometry Techniques 6 1.4 Choice of Mass Spectrometric Techniques and Applications to Measure Isotopic Enrichments in Metabolic Studies 26 1.5 Conclusion and Future Perspectives 30 References 32 2 Stable Isotope Technology 45 Dewi van Harskamp, Johannes B. van Goudoever, and Henk Schierbeek 2.1 History 45 2.2 Definition 45 2.3 Safety 46 2.4 Stable Isotopes and Natural Abundances 47 2.5 Stable Isotope Selection 48 2.6 Single or Multiple Label Selection 49 2.7 Precursor Model 49 2.8 Simultaneous Infusion 49 2.9 Infusion Techniques 50 2.10 Steady State 52 2.11 Pool Selection 52 2.12 Pool Models 53 2.13 Flux: Synthesis and Breakdown 55 2.14 Nitrogen Balance 57 2.15 Doubly LabeledWater Method 57 2.16 Whole-body Protein Synthesis 58 2.17 Specific Protein Synthesis 58 2.18 Calculations 59 2.19 Considerations and Drawbacks of Isotopic Tracers 62 2.20 Conclusion 63 References 63 3 Stable Isotopes in Nutritional and Pediatric Research 67 Willemijn E. Corpeleijn and Johannes B. van Goudoever 3.1 Introduction 67 3.2 Ethical Aspects 69 3.3 Applications of Stable Isotopes in Nutritional and Pediatric Research 70 3.4 Conclusion 78 References 78 4 Early-Life Nutrition and Stable Isotope Techniques 81 Stefanie M.P. Kouwenhoven and Marita deWaard 4.1 Introduction 81 4.2 Breast Milk versus Infant Formula 81 4.3 Techniques to Monitor Milk Intake 82 4.4 Body Composition in Term and Preterm Infants 86 4.5 Amino Acid Requirement 86 4.6 Clinical Applications 87 4.7 Additional Applications 95 4.8 Discussion 98 4.9 Conclusion 99 4.10 Future Perspectives 99 References 100 5 Assessment of Amino Acid Requirement in Children Using Stable Isotopes 108 Femke Maingay-de Groof and Henk Schierbeek 5.1 Introduction 108 5.2 Nutrient Needs and Definitions 109 5.3 Methods to Determine Requirements 111 5.4 Isotopic Tracer Methods 112 5.5 Existing Methods to Determine Amino Acid Requirement for Neonates 114 5.6 Use of the IAAO Method in the Pediatric Population 115 5.7 Necessity for Performing the Study 117 5.8 Biochemistry 117 5.9 Available AnalyticalMethods 120 5.10 Clinical Application 120 5.11 Analysis and Calculations 125 5.12 Results 125 5.13 Statistical Analysis 128 5.14 Discussion 129 5.15 Conclusion 131 5.16 Future Perspectives 132 References 132 6 Metabolism of Glutamine, Citrulline, and Arginine-- Stable Isotopes Analyzing the Intestinal Renal Axis 139 Nikki Buijs, Saskia J.H. Brinkmann, Gerdien C. Ligthart-Melis, and Henk Schierbeek 6.1 Introduction 139 6.2 Biochemistry 142 6.3 Isotopic Model 146 6.4 Study Design 148 6.5 Mass Spectrometry Methods 151 6.6 Clinical Applications 155 6.7 Calculations 158 6.8 Discussion and Future Perspectives 161 References 167 7 Applications in Fat Absorption andMetabolism 175 Dirk-Jan Reijngoud and Henkjan J. Verkade 7.1 Introduction 175 7.2 Biochemistry of Fat Absorption 176 7.3 Isotope Model 178 7.4 Study Design/Infusion Protocols 179 7.5 Analytical Equipment 181 7.6 Analytical Conditions 181 7.7 Accuracy and Precision 183 7.8 Calculations 184 7.9 Clinical Applications 187 7.10 Future Perspectives 191 References 193 8 Materno-Fetal Lipid Kinetics 197 Elvira Larque, Hans Demmelmair, and Berthold Koletzko 8.1 Introduction 197 8.2 Biochemistry of Placental Lipid Transport 198 8.3 Investigation of Fatty Acid Metabolism Using Stable Isotopes 200 8.4 Mass Spectrometry Methods 202 8.5 Clinical Studies with Fatty Acids Labeled with Stable Isotopes in Healthy and Complicated Pregnancies 203 8.6 Calculations 207 8.7 Future Perspectives 209 Acknowledgments 210 References 210 9 Stable Isotope Applications in Human In Vivo Placental and Fetal Research 213 Chris H.P. van den Akker 9.1 Introduction 213 9.2 Investigation of FetalMetabolism Using Stable Isotopes 214 9.3 Study Designs and Models 215 9.4 Infusion Protocols and Clinical Applications 216 9.5 Necessary Additional Clinical Parameters to be Analyzed 218 9.6 Necessary Analytical Mass-Spectrometry Equipment and Analytical Conditions 218 9.7 Calculations 219 9.8 Future Perspectives 222 References 222 10 Obesity 225 Margriet Veldhorst and Henk Schierbeek 10.1 Introduction 225 10.2 Singly and Doubly LabeledWater 226 10.3 Substrate Oxidation 237 10.4 Glucose Metabolism 238 10.5 Fat Metabolism 239 10.6 Protein Turnover 242 10.7 Calculations 246 10.8 Discussion and Future Perspectives 249 References 250 11 Inborn Errors of Metabolism 258 Hidde H. Huidekoper, Frits A.Wijburg, and Ronald J.A.Wanders 11.1 Introduction 258 11.2 Stable Isotope Techniques 260 11.3 Analytical Equipment and Methods 267 11.4 Study Protocol: Quantifying Endogenous Galactose Production 269 11.5 Calculations 271 11.6 Discussion 276 11.7 Future Perspectives 277 References 278 12 Renal Disease and Dialysis 284 Gregorio P.Milani, Sander F. Garrelfs, and Michiel J.S. Oosterveld 12.1 Introduction 284 12.2 Total BodyWater and Its Distribution 286 12.3 Protein Metabolism in Chronic Kidney Disease 291 12.4 Dialysis Metabolic Consequences and Nutrient Losses 293 12.5 Primary Hyperoxalurias 295 12.6 Clinical Applications 298 12.7 Calculations 303 12.8 Discussion 308 12.9 Future Perspectives 310 References 310 13 Application in Oxidative Stress and Glutathione Metabolism in Preterm Infants 320 Denise Rook and Henk Schierbeek 13.1 Introduction 320 13.2 Biochemistry/Model 321 13.3 Guidelines and Safety Procedures 323 13.4 Mass Spectrometry Methods 323 13.5 Materials and Methods 324 13.6 Clinical Application (A Practical Example of a Study Protocol) 327 13.7 Calculations 329 13.8 Discussion and Future Perspectives 330 References 331 14 Nutrient Digestion and Absorption During Intestinal Malfunction and Diseases 336 Margot Fijlstra 14.1 Introduction 336 14.2 Clinical Application 340 References 357 Index 365.
  • (source: Nielsen Book Data)9781118858776 20170403
A guide for scientists, pediatricians and students involved in metabolic studies in pediatric research * Addresses the availability of modern analytical techniques and how to apply these techniques in metabolic studies * Covers the whole range of available mass spectrometric techniques used for metabolic studies including Stable Isotope Methodology * Presents the relevance of mass spectrometry and stable isotope methodology in pediatric research covering applications in Nutrition, Obesity, Metabolic Disorders, and Kidney Disorders * Focuses on the interactions between nutrients and the endogenous metabolism within the body and how these factors affect the health of a growing infant.
(source: Nielsen Book Data)9781118858776 20170403
1 online resource.
  • Contemporary Protein Analysis by Ion Mobility Mass Spectrometry / Johannes PC Vissers, James I Langridge
  • High-Resolution Accurate Mass Orbitrap and Its Application in Protein Therapeutics Bioanalysis / Hongxia Wang, Patrick Bennett 
  • Current Methods for the Characterization of Posttranslational Modifications in Therapeutic Proteins Using Orbitrap Mass Spectrometry / Zhiqi Hao, Qiuting Hong, Fan Zhang, Shiaw-Lin Wu, Patrick Bennett
  • Macro- to Micromolecular Quantitation of Proteins and Peptides by Mass Spectrometry / Suma Ramagiri, Brigitte Simons, Laura Baker
  • Peptide and Protein Bioanalysis Using Integrated Column-to-Source Technology for High-Flow Nanospray / Shane R Needham, Gary A Valaskovic 
  • Targeting the Right Protein Isoform: Mass Spectrometry-Based Proteomic Characterization of Alternative Splice Variants / Jiang Wu
  • The Application of Immunoaffinity-Based Mass Spectrometry to Characterize Protein Biomarkers and Biotherapeutics / Bradley L Ackermann, Michael J Berna
  • Semiquantification and Isotyping of Antidrug Antibodies by Immunocapture-LC/MS for Immunogenicity Assessment / Jianing Zeng, Hao Jiang, Linlin Luo
  • Mass Spectrometry-Based Assay for High-Throughput and High-Sensitivity Biomarker Verification / Xuejiang Guo, Keqi Tang
  • Monitoring Quality of Critical Reagents Used in Ligand Binding Assays with Liquid Chromatography Mass Spectrometry (LC-MS) / Brian Geist, Adrienne Clements-Egan, Tong-Yuan Yang
  • Application of Liquid Chromatography-High Resolution Mass Spectrometry in the Quantification of Intact Proteins in Biological Fluids / Stanley (Weihua) Zhang, Jonathan Crowther, Wenying Jian
  • LC-MS/MS Bioanalytical Method Development Strategy for Therapeutic Monoclonal Antibodies in Preclinical Studies / Hongyan Li, Timothy Heath, Christopher A James
  • Generic Peptide Strategies for LC-MS/MS Bioanalysis of Human Monoclonal Antibody Drugs and Drug Candidates / Michael T Furlong
  • Mass Spectrometry-Based Methodologies for Pharmacokinetic Characterization of Antibody Drug Conjugate Candidates During Drug Development / Yongjun Xue, Priya Sriraman, Matthew V Myers, Xiaomin Wang, Jian Chen, Brian Melo, Martha Vallejo, Stephen E Maxwell, Sekhar Surapaneni
  • Sample Preparation Strategies for LC-MS Bioanalysis of Proteins / Long Yuan, Qin C Ji
  • Characterization of Protein Therapeutics by Mass Spectrometry / Wei Wu, Hangtian Song, Thomas Slaney, Richard Ludwig, Li Tao, Tapan Das.
Presents Practical Applications of Mass Spectrometry for Protein Analysis and Covers Their Impact on Accelerating Drug Discovery and Development * Covers both qualitative and quantitative aspects of Mass Spectrometry protein analysis in drug discovery * Principles, Instrumentation, Technologies topics include MS of peptides, proteins, and ADCs , instrumentation in protein analysis, nanospray technology in MS protein analysis, and automation in MS protein analysis * Details emerging areas from drug monitoring to patient care such as Identification and validation of biomarkers for cancer, targeted MS approaches for biomarker validation, biomarker discovery, and regulatory perspectives * Brings together the most current advances in the mass spectrometry technology and related method in protein analysis.
(source: Nielsen Book Data)9781118605196 20170621
1 online resource.
EBSCOhost Access limited to 1 user
1 online resource (793 pages) : illustrations.
  • What are the structures of the octet rule obeying all-carbon species Cx (2 <= x <= 7 and Larger x)?: a pedagogical, mathematical, and pictorial study / Kori D. McDonald, Evelyn O. Ojo, Joel F. Liebman
  • Self organizing carbon structures: tight binding molecular dynamics calculations / István László, Ibolya Zsoldos, Dávid Fülep
  • Layered double hydroxides-based materials as oxidation catalysts / Ioan-Cezar Marcu [and 3 others]
  • Characteristic polynomial in assessment of carbon-nano structures / Sorana D. Bolboaca, Lorentz Jäntschi
  • Case studies in the challenge of properties design at nanoscale: bonding mechanisms and causal relationship / Marilena Ferbinteanu, Harry Ramanantoanina, Fanica Cimpoesu
  • Main allotropes of carbon: a brief review / Zahra Khalaj, Majid Monajjemi, Mircea V. Diudea
  • Space of nanoworld / G. V. Zhizhin, M. V. Diudea
  • Effects of spin orbit interaction on optical properties for quantum dot and quantum wire / Manoj Kumar, Pradip Kumar Jha, Aranya B. Bhattacherjee
  • Quantum dots searching for bondots: towards sustainable sensitized solar cells / Mihai V. Putz, Marina A. Tudoran, Marius C. Mirica
  • Bondonic electrochemistry: basic concepts and sustainable prospects / Mihai V. Putz, Marina A. Tudoran, Marius C. Mirica
  • Sustainable design of photovoltaics: devices and quantum information / Mihai V. Putz [and 8 others]
  • Up-converting nanoparticles: promising markers for biomedical applications / Livia Petrescu [and 3 others]
  • A theoretical study of the refractive index of KDP crystal doped with TiO2 nanoparticles / Volodymyr Krasnoholovets
  • Sustainable nanosystem development for mass spectrometry: applications in proteomics and glycomics / Laurentiu Popescu, Adrian C. Robu, Alina D. Zamfir
  • Graphene and fullenene clusters: molecular polarizability and ion-di/graphene associations / Francisco Torrens, Gloria Castellano
  • Entropy of nanostructures: topological effects on Schottky vacancies concentration in graphenic bidimensional HC(N) lattices / Ottorino Ori, Franco Cataldo, Mihai V. Putz
  • Atlas of [rho], [rho]E, and TM-EC for Fullerenes isomers / Fatemeh Koorepazan-Moftakhar [and 3 others]
  • Developing sustainability: some scientific and ethical issues / Margherita Venturi.
Global economic demands and population surges have led to dwindling resources and problematic environmental issues. As the climate and its natural resources continue to struggle, it has become necessary to research and employ new forms of sustainable technology to help meet the growing demand. Sustainable Nanosystems Development, Properties, and Applications features emergent research and theoretical concepts in the areas of nanotechnology, photovoltaics, electrochemistry, and materials science, as well as within the physical and environmental sciences. Highlighting progressive approaches and utilization techniques, this publication is a critical reference source for researchers, engineers, students, scientists, and academicians interested in the application of sustainable nanotechnology.
(source: Nielsen Book Data)9781522504924 20161213
1 online resource.
  • Overview. Overview of Targeted Quantitation of Biomarkers and Its Applications / Naidong Weng
  • Translational Application of Biomarkers / Ray Bakhtiar
  • Current Regulatory Guidance Pertaining Biomarker Assay Establishment and Industrial Practice of Fit-for-Purpose and Tiered Approach / Naidong Weng
  • Modern Liquid Chromatography and Mass Spectrometry for Targeted Biomarker Quantitation / Wenying Jian
  • Comparison Between LC-MS and Ligand-Binding Assay Approaches for Biomarker Quantification / QingQing Wang, Lili Guo, Ian A Blair
  • Sample Preparation Methods for Targeted Biomarker Quantification by LC-MS / Shichen Shen, Bo An, Jun Qu
  • Overcome the Endogenous Levels in Biomarker Quantitation Using LC-MS / Guowen Liu
  • Challenges and Approaches. Sample Collection for Targeted Biomarker Quantitation by LC-MS / Yuzhong Deng, Xiaorong Liang
  • Nonspecific Binding in LC-MS Bioanalysis / Aimin Tan, John C Fanaras
  • Strategies for Improving Sensitivity for Targeted Quantitation by LC-MS / Long Yuan, Qin C Ji
  • Strategies to Improve Specificity for Targeted Biomarker Quantitation by LC-MS / Yuan-Qing Xia, Jeffrey D Miller
  • Biomarker Quantitation Using Relative Approaches / Shane M Lamos, Katrina E Wiesner
  • Applications. Targeted Quantification of Amino Acid Biomarkers Using LC-MS / Barry R Jones, Raymond F Biondolillo, John E Buckholz
  • Targeted Quantification of Peptide Biomarkers / Lieve Dillen, Marc De Meulder, Tom Verhaeghe
  • Targeted Protein Biomarker Quantitation by LC-MS / Yongle Pang, Chuan Shi, Wenying Jian
  • Glycoprotein Biomarkers / Shuwei Li, Stefani N Thomas, Shuang Yang
  • Targeted Lipid Biomarker Quantitation Using Liquid Chromatography-Mass Spectrometry (LC-MS) / Ashkan Salamatipour, Ian A Blair, Clementina Mesaros
  • Targeted LC-MS Quantification of Androgens and Estrogens for Biomarker Development / Daniel Tamae
  • Steroid Biomarkers / Mike (Qingtao) Huang, Shefali Patel, Zhongping (John) Lin
  • Bile Acids as Biomarkers / Clara John, Philipp Werner, Joerg Heeren, Markus Fischer
  • Biomarkers for Vitamin Status and Deficiency / Stanley (Weihua) Zhang, Jonathan Crowther
  • Quantitation of Acyl-Coenzyme A Thioesters as Metabolic Biomarkers / Nathaniel Snyder
  • Neurotransmitter Biomarkers / Guodong Zhang
  • Targeted Quantification of Carbohydrate Biomarkers Using LC-MS / Cong Wei, Hong Gao
  • Nucleoside/Nucleotide Biomarkers / Guodong Zhang
  • LC-MS of RNA Biomarkers / Michael G Bartlett, Babak Basiri, Ning Li.
1 online resource.
  • Employing 'second generation' matrices.- (MA)LDI MS mass spectrometry imaging at high specificity and sensitivity.- Techniques for fingermark analysis using MALDI MS - a practical overview.- Whole/Intact Cell MALDI MS Biotyping in Mammalian Cell Analyis.- MALDI biotyping for microorganism identification in clinical microbiology.- Future applications of MALDI-TOF MS in microbiology.- MALDESI: Fundamentals, direct analysis, and MS imaging.- Microprobe MS Imaging of Live Tissues, Cells, and Bacterial Colonies using LAESI.- Efficient production of multiply charged MALDI ions.- Food Authentication by MALDI MS - MALDI-TOF MS Analysis of Fish Species.- Quantitative MALDI MS using Ionic Liquid Matrices.- Disease profiling by MALDI MS analysis of biofluids.- Ionic Liquids and other liquid matrices for sensitive MALDI MS analysis.- Coupling liquid MALDI MS to liquid chromatography.
  • (source: Nielsen Book Data)9783319048185 20160619
This book covers the state-of-the-art of modern MALDI (matrix-assisted laser desorption/ionization) and its applications. New applications and improvements in the MALDI field such as biotyping, clinical diagnosis, forensic imaging, and ESI-like ion production are covered in detail. Additional topics include MS imaging, biotyping/speciation and large-scale, high-speed MS sample profiling, new methods based on MALDI or MALDI-like sample preparations, and the advantages of ESI to MALDI MS analysis. This is an ideal book for graduate students and researchers in the field of bioanalytical sciences. This book also: * Showcases new techniques and applications in MALDI MS * Demonstrates how MALDI is preferable to ESI (electrospray ionization) * Illustrates the pros and cons associated with biomarker discovery studies in clinical proteomics and the various application areas, such as cancer proteomics.
(source: Nielsen Book Data)9783319048185 20160619
1 online resource (16 p.) : digital, PDF file.
Overcoming the natural recalcitrance of lignocellulosic biomass is necessary in order to efficiently convert biomass into biofuels or biomaterials and many times this requires some type of chemical pretreatment and/or biological treatment. While bulk chemical analysis is the traditional method of determining the impact a treatment has on biomass, the chemistry on the surface of the sample can differ from the bulk chemistry. Specifically, enzymes and microorganisms bind to the surface of the biomass and their efficiency could be greatly impacted by the chemistry of the surface. Therefore, it is important to study and understand the chemistry of the biomass at the surface. Time-of- flight secondary ion mass spectrometry (ToF-SIMS) is a powerful tool that can spectrally and spatially analyze the surface chemistry of a sample. This review discusses the advances in understanding lignocellulosic biomass surface chemistry using the ToF-SIMS by addressing the instrument parameters, biomass sample preparation, and characteristic lignocellulosic ion fragmentation peaks along with their typical location in the plant cell wall. Furthermore, the use of the ToF-SIMS in detecting chemical changes due to chemical pretreatments, microbial treatments, and physical or genetic modifications is discussed along with possible future applications of the instrument in lignocellulosic biomass studies.
1 online resource.
  • Introduction / Rebecca Pferdehirt, Florian Gnad, Jennie R Lill
  • Identification and Analysis of Protein Phosphorylation by Mass Spectrometry / Dean E McNulty, Timothy W Sikorski, Roland S Annan
  • Analysis of Protein Glycosylation by Mass Spectrometry / David J Harvey
  • Protein Acetylation and Methylation / Caroline Evans
  • Tyrosine Nitration / Xianquan Zhan, Ying Long, Dominic M Desiderio
  • Mass Spectrometry Methods for the Analysis of Isopeptides Generated from Mammalian Protein Ubiquitination and SUMOylation / Navin Chicooree, Duncan L Smith
  • The Deimination of Arginine to Citrulline / Andrew J Creese, Helen J Cooper
  • Glycation of Proteins / Naila Rabbani, Paul J Thornalley
  • Biological Significance and Analysis of Tyrosine Sulfation / Eva Klement, Eva Hunyadi-Guly's, Katalin F Medzihradszky
  • The Application of Mass Spectrometry for the Characterization of Monoclonal Antibody-Based Therapeutics / Rosie Upton, Kamila J Pacholarz, David Firth, Sian Estdale, Perdita E Barran.
-Covers all major modifications, including phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation -Discussion of the chemistry behind each modification, along with key methods and references -Contributions from some of the leading researchers in the field -A valuable reference source for all laboratories undertaking proteomics, mass spectrometry and post-translational modification research.
xii, 269 pages : illustrations, map ; 24 cm
  • List of Contributors ix Preface xi 1 Principles and Applications of Ion Chromatography 1 Rajmund Michalski 1.1 Principles of Ion Chromatography, 1 1.1.1 Introduction, 1 1.1.2 Stationary Phases, 6 1.1.3 Eluents, 13 1.1.4 Suppressors, 16 1.1.5 Detection Methods, 18 1.2 Ion Chromatography Applications, 23 1.2.1 Speciation Analysis with the Hyphenated Methods of IC-ICP-MS and IC-MS, 29 1.3 Sample Preparation for Ion Chromatography, 32 1.4 Selected Methodological Aspects of Ion Determination with Ion Chromatography, 34 1.5 Ion Chromatography Development Perspectives, 37 1.6 References, 37 2 Mass Spectrometric Detectors for Environmental Studies 47 Maria Balcerzak 2.1 Introduction, 47 2.2 Mass Spectrometric Detectors, 49 2.2.1 Ionization Methods, 50 2.2.2 Mass Analyzers, 58 Acknowledgments, 62 2.3 References, 62 3 High-Performance Liquid Chromatography Coupled to Inductively Coupled Plasma MS/Electrospray Ionization MS 79 Jurgen Mattusch 3.1 Separation Principles, 79 3.1.1 Ion Chromatography (Anion/Cation Exchange, Mixed Mode), 80 3.1.2 High-Performance Liquid Chromatography (Reversed-Phase Mode, HILIC), 81 3.1.3 Size Exclusion Chromatography (SEC) (Gel Filtration Chromatography, GFC), 82 3.2 Detection Principles, 83 3.2.1 Common Detection in IC: Conductivity, UV Vis, Electrochemical Detection, 83 3.2.2 Element Specific Detection, 83 3.3 Hyphenated Techniques, 87 3.3.1 HPLC(IC) ICP-MS, 87 3.4 HPLC(IC) ICP-MS/ESI-MS, 90 3.4.1 Fundamentals, 90 3.4.2 Methodology of Data Evaluation, 90 3.4.3 Technical Requirements, 91 3.5 Applications and Conclusion, 91 3.6 References, 102 4 Application of IC-MS in Organic Environmental Geochemistry 109 Klaus Fischer 4.1 Introduction, 109 4.2 Carboxylic Acids, 114 4.2.1 Molecular Structure, Molecular Interaction Potential, and Chromatographic Retention, 114 4.2.2 Environmental Analysis of Carboxylic Acids by Ion Exclusion Chromatography Mass Spectrometry (HPICE-MS), 116 4.2.3 Environmental Analysis of Carboxylic Acids by Ion-Exchange Chromatography Mass Spectrometry (HPI-EC-MS), 124 4.3 Carbohydrates, 135 4.3.1 Structural Diversity and Ion Chromatographic Behavior, 135 4.3.2 Environmental Analysis of Carbohydrates by Various IC-MS Methods, 136 4.4 Amines and Amino Acids, 143 4.5 Trends and Perspectives, 144 4.6 References, 145 5 Analysis of Oxyhalides and Haloacetic Acids in Drinking Water Using IC-MS and IC-ICP-MS 152 Koji Kosaka 5.1 Introduction, 152 5.2 Source of Oxyhalides and HAAs, 154 5.3 Analysis of Oxyhalides and HAAs, 158 5.3.1 Suppressed IC-MS, 158 5.3.2 Nonsuppressed IC-MS and LC-MS, 162 5.3.3 IC-ICP-MS, 165 5.4 Application for Monitoring of Oxyhalides and HAAs in Drinking Water, 166 5.4.1 Oxyhalides, 166 5.4.2 HAAs, 171 Summary, 171 5.5 References, 172 6 Analysis of Various Anionic Metabolites in Plant and Animal Material by IC-MS 178 Adam Konrad Jagielski and Michal Usarek 6.1 Introduction, 178 6.2 Optimization of HPIC and Ms Settings, 179 6.2.1 HPIC Settings, 179 6.2.2 MS Settings, 183 6.2.3 HPIC-MS Settings, 185 6.2.4 Extraction of Metabolites from Cells and Tissues, 189 6.3 Application of the Method in Analysis of Metabolites in Plant and Animal Material, 191 6.3.1 Analysis of Metabolites from Cell Cultures (Primary Cultures as well as Established Cell Lines), 192 6.3.2 Analysis of Metabolites from Solid Tissues, 192 6.3.3 Extraction of Metabolites from Plants, 194 6.4 Conclusions, 196 6.5 References, 197 7 Analysis of Perchlorate Ion in Various Matrices Using Ion Chromatography Hyphenated with Mass Spectrometry 199 Jay Gandhi 7.1 Introduction, 199 7.2 Precautions Unique to Ion Chromatography Mass Spectrometry, 200 7.2.1 Instrumental and Operating Parameters, 201 7.3 Results and Discussion, 204 Acknowledgment, 209 7.4 References, 209 8 Sample Preparation Techniques for Ion Chromatography 210 Wolfgang Frenzel and Rajmund Michalski 8.1 Introduction, 210 8.2 When and Why is Sample Preparation Required in Ion Chromatography? 213 8.3 Automation of Sample Preparation (IN-LINE Techniques), 215 8.4 Sample Preparation Methods, 217 8.4.1 Filtration and Ultrafiltration, 219 8.4.2 Solid-Phase Extraction (SPE), 220 8.4.3 Liquid Liquid Extraction, 225 8.4.4 Gas-Phase Separations, 226 8.4.5 Precipitation, 226 8.4.6 Membrane-Based Separations and Sample Treatment, 227 8.5 Trace Analysis and Preconcentration for Ion Chromatographic Analysis, 238 8.5.1 Preconcentration Using SPE, 239 8.5.2 Membrane-Based In-Line Preconcentration, 241 8.6 In-Line Preseparations Using Two-Dimensional Ion Chromatography (2D-IC), 243 8.7 Sample Preparation of Solid Samples, 244 8.7.1 Dissolution and Aqueous or Acid Extraction, 246 8.7.2 Wet-Chemical Acid Digestions, 247 8.7.3 UV Photolytic Digestion, 248 8.7.4 Fusion Methods, 249 8.7.5 Dry Ashing and Combustion Methods, 249 8.8 Air Analysis Using Ion Chromatography Application to Gases and Particulate Matter, 251 8.9 Postcolumn Eluent Treatment Prior to Ms Detection, 255 8.10 Concluding Remarks, 257 8.11 References, 258 Index 267.
  • (source: Nielsen Book Data)9781118862001 20160808
Introduces the reader to the field of ion chromatography, species analysis and hyphenated methods IC-MS and IC-ICP-MS including the theory and theirs applications * Covers the importance of species analysis and hyphenated methods in ion chromatography * Includes practical applications of IC-MS and IC-ICP-MS in environmental analysis * Details sample preparation methods for ion chromatography * Discusses hyphenated methods IC-MS and IC-ICP-MS used in determining both the total element contents and its elements * Details speciation analysis used in studying biochemical cycles of selected chemical compounds; determining toxicity and ecotoxicity of elements; food and pharmaceuticals quality control; and in technological process control and clinical analytics.
(source: Nielsen Book Data)9781118862001 20160808
Science Library (Li and Ma)
1 online resource (viii, 336 pages) : illustrations (some color)
In the last quarter century, advances in mass spectrometry (MS) have been at the forefront of efforts to map complex biological systems including the human metabolome, proteome, and microbiome. All of these developments have allowed MS to become a well-established molecular level technology for microbial characterization. MS has demonstrated its considerable advantage as a rapid, accurate, and cost-effective method for microbial identification, compared to conventional phenotypic techniques. In the last several years, applications of MS for microbial characterization in research, clinical microbiology, counter-bioterrorism, food safety, and environmental monitoring have been documented in thousands of publications. Regulatory bodies in Europe, the US, and elsewhere have approved MS-based assays for infectious disease diagnostics. As of mid-2015, more than 3300 commercial MS systems for microbial identification have been deployed worldwide in hospitals and clinical labs. While previous work has covered broader approaches in using MS to characterize microorganisms at the species level or above, this book focuses on strain-level and subtyping applications. In thirteen individual chapters, innovators, leaders and practitioners in the field from around the world have contributed to a comprehensive overview of current and next-generation approaches for MS-based microbial characterization at the subspecies and strain levels. Chapters include up-to-date reference lists as well as web-links to databases, recommended software, and other useful tools. The emergence of new, antibiotic-resistant strains of human or animal pathogens is of extraordinary concern not only to the scientific and medical communities, but to the general public as well. Developments of novel MS-based assays for rapid identification of strains of antibiotic-resistant microorganisms are reviewed in the book as well. Microbiologists, bioanalytical scientists, infectious disease specialists, clinical laboratory and public health practitioners as well as researchers in universities, hospitals, government labs, and the pharmaceutical and biotechnology industries will find this book to be a timely and valuable resource.
1 online resource (Article No. 22321 ) : digital, PDF file.
In this study, we report the atomic-scale analysis of biological interfaces using atom probe tomography. Embedding the protein ferritin in an organic polymer resin lacking nitrogen provided chemical contrast to visualize atomic distributions and distinguish organic-organic and organic-inorganic interfaces. The sample preparation method can be directly extended to further enhance the study of biological, organic and inorganic nanomaterials relevant to health, energy or the environment.
1 online resource.
  • Detection in Capillary Electrophoresis - An Introduction Electrospray Ionization Interface Development for Capillary Electrophoresis-Mass Spectrometry Sheath Liquids in CE-MS: Role, Parameters, and Optimization Recent Developments of Microchip Capillary Electrophoresis Coupled with Mass Spectrometry On-line Electrophoretic, Electrochromatographic, and Chromatographic Sample Concentration in CE-MS CE-MS in Drug Analysis and Bioanalysis Intact Protein Analysis by Capillary Electrophoresis - Mass Spectrometry CE-MS in Food Analysis and Foodomics CE-MS in Forensic Sciences with Focus on Forensic Toxicology CE-MS in Metabolomics CE-MS for Clinical Proteomics and Metabolomics: Strategies and Applications.
  • (source: Nielsen Book Data)9783527693832 20170313
This monograph offers the reader a complete overview on both principles and applications of CE-MS. Starting with an introductory chapter on detection in CE, also related and more specialized techniques such as electrophoretic and chromatographic preconcentration are discussed. A special emphasis is put on CE-MS interfaces, which are described in detail. In a separate chapter, attention is paid to sheath-liquid interfacing. The developments and possibilities of microchip CE-MS are also described. Applications to all relevant areas are discussed in distinct chapters, each written by experts in the respective fields. Besides applications in pharmaceutical analysis and bioanalysis, recent implementations in food science, forensic analysis, analysis of intact proteins, metabolomics and proteomics are highlighted. MS is a perfectly appropriate detection system for CE, as efficient separation is coupled to sensitive and selection detection. Moreover, MS can provide structure information on the separated compounds. CE-MS has now been developed into a strong hyphenated system complementary to LC-MS. This monograph is an unique source of knowledge for everyone dealing with and interested in CE-MS.
(source: Nielsen Book Data)9783527693832 20170313
1 online resource Digital: text file; PDF.
  • Introduction to Capillary Electrophoresis-Mass Spectrometry.- Coated Capillaries for CE-MS of Therapeutic Protein.- Intact Mass Analysis of Monoclonal Antibodies by Capillary Electrophoresis-Mass Spectrometry.- Separation and Characterization of Proteins and Peptides in Biological Fluids using CE-MS.- Host Cell Protein Analysis using CE-MS.- Antibody PTM Analysis using CE-MS.- Characterization of Intact Therapeutic Proteins and Protein Subunits using CE-MS Platform.
  • (source: Nielsen Book Data)9783319462387 20170117
This book covers the latest developments in capillary electrophoresis-mass spectrometry for the analysis of therapeutic proteins. The application of capillary electrophoresis-mass spectrometry (CE-MS) coupling technology in the analysis of recombinant therapeutic proteins is detailed thoroughly. Specific topics include recent developments in coupling capillary electrophoresis with mass spectrometry for the quality control of monoclonal antibody therapeutics, top-down analysis of monoclonal antibody using the CE-MS platform, and detection of host cell protein impurities. Comprehensive characterization of antibody-drug conjugates (ADCs) by coupling capillary electrophoresis with mass spectrometry is also covered. This is an ideal book for scientists in the life science and biopharmaceutical industry who are working on characterizing the PTMs of monoclonal antibodies, as well as graduate students and researchers in the separation science and biological mass spectrometry fields.
(source: Nielsen Book Data)9783319462387 20170117

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