Book
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
Book
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
Biology Library (Falconer)
Book
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.
Book
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.
Collection
Undergraduate Theses, Department of Biology, 2015-2016
Population growth places great strain on our natural resources, bringing to the forefront the pressing problems such as limited food supplies. One way to address this problem is by improving plant photosynthetic efficiency, resulting in increased plant productivity and higher crop yields. To study photosynthesis and carbon concentration, we use the model organism Chlamydomonas reinhardtii, a single-celled green alga with an inducible carbon concentrating mechanism (CCM) that allows it to perform efficient photosynthesis: our long-term goal is to introduce the algal CCM into higher land plants, which would reduce photorespiration and enhance photosynthesis. It is necessary, therefore, to identify the key components of the CCM and to understand their molecular interactions in order to transfer this mechanism into crop plants. To this end, we have developed a pipeline for large-scale characterization of the algal CCM components and map how these components function together. With fluorescent and affinity tagging coupled to immunoprecipitation (IP) and mass spectrometry to explore these mechanisms, we took the localization data for 40 putative photosynthesis and CCM components to present 381 confident interactions between the proteins involved. The developed pipeline and the foundational knowledge reported here provide valuable tools for continuing work towards bioengineering of the CCM.
Book
online resource (xv, 333 pages) : illustrations (some color)
  • Mass spectrometry in clinical laboratory : applications in biomolecular analysis / Uttam Garg and Yan Victoria Zhang
  • Quantification of free carnitine and acylcarnitines in plasma or serum using HPLC/MS/MS / David Scott, Bryce Heese, and Uttam Garg
  • Quantification of arginine and its methylated derivatives in plasma by high-performance liquid chromatography tandem mass spectrometry (LC-MS/MS) / Faye B. Vicente ... [et al.]
  • Quantitation of albumin in urine by liquid chromatography tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of aldosterone in serum or plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantification of five clinically important amino acids by HPLC-Triple TOF 5600 based on pre-column double derivatization method / Shuang Deng, David Scott, and Uttam Garg
  • Sensitive, simple, and robust nano-liquid chromatography-mass spectrometry method for amyloid protein subtyping / Drew Payto, Courtney Heideloff, and Sihe Wang
  • Quantitation of ubiquinone (coenzyme Q10) in serum/plasma using liquid chromatography electrospray tandem mass spectrometry (ESI-LC-MS/MS) / Richard E. Mathieu Jr. and Catherine P. Riley
  • Quantitative analysis of salivary cortisol using LC-MS/MS / Yan Victoria Zhang
  • Quantification of dihydroxyacetone phosphate (DHAP) in human red blood cells by HPLC-TripleTOF 5600 mass spectrometer / Shuang Deng ... [et al.]
  • Simultaneous quantitation of estradiol and sstrone in serum using liquid chromatography mass spectrometry / Catherine P. Riley, Richard E. Mathieu Jr., and Carmen Wiley
  • Direct measurement of free estradiol in human serum and plasma by equilibrium dialysis-liquid chromatography-tandem mass spectrometry / Julie A. Ray ... [et al.]
  • Quantification of γ-aminobutyric acid in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitation of insulin analogues in serum using immunoaffinity extraction, liquid chromatography, and tandem mass spectrometry / J. Grace Van Der Gugten, Sophia Wong, and Daniel T. Holmes
  • Quantitation of insulin-like growth factor 1 in serum by liquid chromatography high resolution accurate-mass mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of free metanephrines in plasma by liquid chromatography-tandem mass spectrometry / Courtney Heideloff, Drew Payto, and Sihe Wang
  • Quantification of metanephrine and normetanephrine in urine using liquid chromatography-tandem mass spectrometry / Jessica Gabler and Sihe Wang
  • High-throughput analysis of methylmalonic acid in serum, plasma, and urine by LC-MS/MS. Method for analyzing isomers without chromatographic separation / Mark M. Kushnir ... [et al.]
  • Quantitation of 5-methyltetrahydrofolate in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitative organic acids in urine by two dimensional gas chromatography-time of flight mass spectrometry (GCxGC-TOFMS) / Lawrence Sweetman, Paula Ashcraft, and Jeanna Bennett-Firmin
  • High sensitivity measurement of pancreatic polypeptide and its variant in serum and plasma by LC-MS/MS / Hernando Escobar ... [et al.]
  • Quantitation of parathyroid hormone in serum or plasma by liquid chromatography-tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Determination of phenylalanine and tyrosine by high performance liquid chromatography-tandem mass spectrometry / Judy Peat and Uttam Garg
  • Urine purine metabolite determination by UPLC-tandem mass spectrometry / Qin Sun
  • Urine pyrimidine metabolite determination by HPLC tandem mass spectrometry / Qin Sun
  • Quantitation of plasma renin activity in plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantitation of S-adenosylmethionine and S-adenosylhomocysteine in plasma using liquid chromatography electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Simple, high-throughput method for analysis of ceramide, glucosylceramide, and ceramide trihexoside in dried blood spots by LC/MS/MS / Wei-Lien Chuang, Joshua Pacheco, and Kate Zhang
  • Quantification of dehydroepiandrosterone, 11-Deoxycortisol, 17-Hydroxyprogesterone, and testosterone by liquid chromatography-tandem mass spectrometry (LC/MS/MS) / Ada Munar, Clint Frazee, and Uttam Garg
  • Urinary succinylacetone analysis by gas chromatography-mass spectrometry (GC-MS) / Hongjie Chen and Chunli Yu
  • Quantification of 1,25-Dihydroxyvitamin D2 and D3 in serum using liquid chromatography-tandem mass spectrometry / Jonathon Mahlow, Dustin R. Bunch, and Sihe Wang
  • High-throughput serum 25-hydroxy vitamin D testing with automated sample preparation / Judy Stone
  • Quantitation of 25-OH-Vitamin-D2 and 25-OH-Vitamin-D3 in urine using LC-MS/MS / Dean C. Carlow, Ryan C. Schofield, and Michelle Denburg.
Medical Library (Lane)
Book
xv, 333 pages : illustrations (some color) ; 26 cm.
  • Mass spectrometry in clinical laboratory : applications in biomolecular analysis / Uttam Garg and Yan Victoria Zhang
  • Quantification of free carnitine and acylcarnitines in plasma or serum using HPLC/MS/MS / David Scott, Bryce Heese, and Uttam Garg
  • Quantification of arginine and its methylated derivatives in plasma by high-performance liquid chromatography tandem mass spectrometry (LC-MS/MS) / Faye B. Vicente [and others]
  • Quantitation of albumin in urine by liquid chromatography tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of aldosterone in serum or plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantification of five clinically important amino acids by HPLC-Triple TOF 5600 based on pre-column double derivatization method / Shuang Deng, David Scott, and Uttam Garg
  • Sensitive, simple, and robust nano-liquid chromatography-mass spectrometry method for amyloid protein subtyping / Drew Payto, Courtney Heideloff, and Sihe Wang
  • Quantitation of ubiquinone (coenzyme Q10) in serum/plasma using liquid chromatography electrospray tandem mass spectrometry (ESI-LC-MS/MS) / Richard E. Mathieu Jr. and Catherine P. Riley
  • Quantitative analysis of salivary cortisol using LC-MS/MS / Yan Victoria Zhang
  • Quantification of dihydroxyacetone phosphate (DHAP) in human red blood cells by HPLC-TripleTOF 5600 mass spectrometer / Shuang Deng [and others]
  • Simultaneous quantitation of estradiol and sstrone in serum using liquid chromatography mass spectrometry / Catherine P. Riley, Richard E. Mathieu Jr., and Carmen Wiley
  • Direct measurement of free estradiol in human serum and plasma by equilibrium dialysis-liquid chromatography-tandem mass spectrometry / Julie A. Ray [and others]
  • Quantification of γ-aminobutyric acid in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitation of insulin analogues in serum using immunoaffinity extraction, liquid chromatography, and tandem mass spectrometry / J. Grace Van Der Gugten, Sophia Wong, and Daniel T. Holmes
  • Quantitation of insulin-like growth factor 1 in serum by liquid chromatography high resolution accurate-mass mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Quantitation of free metanephrines in plasma by liquid chromatography-tandem mass spectrometry / Courtney Heideloff, Drew Payto, and Sihe Wang
  • Quantification of metanephrine and normetanephrine in urine using liquid chromatography-tandem mass spectrometry / Jessica Gabler and Sihe Wang
  • High-throughput analysis of methylmalonic acid in serum, plasma, and urine by LC-MS/MS. Method for analyzing isomers without chromatographic separation / Mark M. Kushnir [and others]
  • Quantitation of 5-methyltetrahydrofolate in cerebrospinal fluid using liquid chromatography-electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Quantitative organic acids in urine by two dimensional gas chromatography-time of flight mass spectrometry (GCxGC-TOFMS) / Lawrence Sweetman, Paula Ashcraft, and Jeanna Bennett-Firmin
  • High sensitivity measurement of pancreatic polypeptide and its variant in serum and plasma by LC-MS/MS / Hernando Escobar [and others]
  • Quantitation of parathyroid hormone in serum or plasma by liquid chromatography-tandem mass spectrometry / Hemamalini Ketha and Ravinder J. Singh
  • Determination of phenylalanine and tyrosine by high performance liquid chromatography-tandem mass spectrometry / Judy Peat and Uttam Garg
  • Urine purine metabolite determination by UPLC-tandem mass spectrometry / Qin Sun
  • Urine pyrimidine metabolite determination by HPLC tandem mass spectrometry / Qin Sun
  • Quantitation of plasma renin activity in plasma using liquid chromatography-tandem mass spectrometry (LC- MS/MS) / J. Grace Van Der Gugten and Daniel T. Holmes
  • Quantitation of S-adenosylmethionine and S-adenosylhomocysteine in plasma using liquid chromatography electrospray tandem mass spectrometry / Erland Arning and Teodoro Bottiglieri
  • Simple, high-throughput method for analysis of ceramide, glucosylceramide, and ceramide trihexoside in dried blood spots by LC/MS/MS / Wei-Lien Chuang, Joshua Pacheco, and Kate Zhang
  • Quantification of dehydroepiandrosterone, 11-Deoxycortisol, 17-Hydroxyprogesterone, and testosterone by liquid chromatography-tandem mass spectrometry (LC/MS/MS) / Ada Munar, Clint Frazee, and Uttam Garg
  • Urinary succinylacetone analysis by gas chromatography-mass spectrometry (GC-MS) / Hongjie Chen and Chunli Yu
  • Quantification of 1,25-Dihydroxyvitamin D2 and D3 in serum using liquid chromatography-tandem mass spectrometry / Jonathon Mahlow, Dustin R. Bunch, and Sihe Wang
  • High-throughput serum 25-hydroxy vitamin D testing with automated sample preparation / Judy Stone
  • Quantitation of 25-OH-Vitamin-D2 and 25-OH-Vitamin-D3 in urine using LC-MS/MS / Dean C. Carlow, Ryan C. Schofield, and Michelle Denburg.
This volume provides stepwise instructions for the analysis of numerous clinically important analytes by mass spectrometry. Mass spectrometry offers clinical laboratory scientists a number of advantages including increased sensitivity and specificity, multiple component analysis, and no need for specialized reagents. The techniques described are a must for the measurement of many clinically relevant analytes in the fields of drug analysis, endocrinology, and inborn errors of metabolism. Each chapter provides a brief introduction about a specified analyte, followed by detailed instructions on the analytical protocol. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting edge and practical, Clinical Applications of Mass Spectrometry in Biomolecular Analysis: Methods and Protocols is a great resource for clinical laboratory scientists who are already using or thinking of bringing mass spectrometry to their laboratories.
(source: Nielsen Book Data)9781493931811 20160619
Biology Library (Falconer)
Book
xv, 272 pages : illustrations (some color) ; 26 cm.
  • Mass spectrometry in clinical laboratory : applications in therapeutic drug monitoring and toxicology / Uttam Garg and Yan Victoria Zhang
  • Quantitation of flecainide, mexiletine, propafenone, and amiodarone in serum or plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Quantitation of the oral anticoagulants dabigatran, rivaroxaban, apixaban, and warfarin in plasma using ultra-performance liquid chromatography with tandem mass spectrometry (UPLC-MS/MS) / Jaime H. Noguez and James C. Ritchie
  • Simultaneous quantitation of lamotrigine, levetiracetam, 10-Hydroxycarbazepine, topiramate, and zonisamide in serum using HPLC-MS/MS / Dean C. Carlow, Heng Shi, and Ryan C. Schofield
  • Quantification of the triazole antifungal compounds voriconazole and posaconazole in human serum or plasma using liquid chromatography electrospray tandem mass spectrometry (HPLC-ESI-MS/MS) / Alejandro R. Molinelli and Charles H. Rose IV
  • Quantitation of haloperidol, fluphenazine, perphenazine, and thiothixene in serum or plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Quantitation of total buprenorphine and norbuprenorphine in meconium by LC-MS/MS / Stephanie J. Marin and Gwendolyn A. McMillin
  • Quantitation of buprenorphine, norbuprenorphine, buprenorphine glucuronide, norbuprenorphine glucuronide, and naloxone in urine by LC-MS/MS / Stephanie J. Marin and Gwendolyn A. McMillin
  • Simple liquid chromatography tandem mass spectrometry method for quantitation of plasma busulfan / Shuang Deng [and others]
  • High-throughput quantitation of busulfan in plasma using ultrafast solid-phase extraction tandem mass spectrometry (SPE-MS/MS) / Loralie J. Langman [and others]
  • Quantification of 11-carboxy-delta-9-tetrahydrocannabinol (THC-COOH) in meconium using gas chromatography/mass spectrometry (GC/MS) / Judy Peat [and others]
  • Quantitation of carisoprodol and meprobamate in urine and plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Cetirizine quantification by high-performance liquid chromatography tandem mass spectrometry (LC-MS/MS) / Ada Munar [and others]
  • Quantification of docetaxel in serum using turbulent flow liquid chromatography electrospray tandem mass spectrometry (TFC-HPLC-ESI-MS/MS) / Christopher A. Crutchfield, Mark A. Marzinke, and William A. Clarke
  • Comprehensive urine drug screen by gas chromatography/mass spectrometry (GC/MS) / Bheemraj Ramoo [and others]
  • Broad-spectrum drug screening using liquid chromatography-hybrid triple-quadrupole linear ion trap mass spectrometry / Judy Stone
  • High-resolution mass spectrometry for untargeted drug screening / Alan H.B. Wu and Jennifer Colby
  • Quantitation of ethyl glucuronide and ethyl sulfate in urine using liquid chromatography-tandem mass spectrometry (LC-MS/MS) / Matthew H. Slawson and Kamisha L. Johnson-Davis
  • Quantification of hydroxychloroquine in blood using turbulent flow liquid chromatography-tandem mass spectrometry (TFLC-MS/MS) / Allison B. Chambliss, Anna K. Füzéry, and William A. Clarke
  • Quantification of iohexol in serum by high-performance liquid chromatography-tandem mass spectrometry (LC- MS/MS) / Faye B. Vicente [and others]
  • Quantitation of teriflunomide in human serum/plasma across a 40,000-fold concentration range by LC/MS/MS / Geoffrey S. Rule, Alan L. Rockwood, and Kamisha L. Johnson-Davis
  • Determination of menthol in plasma and urine by gas chromatography/mass spectrometry (GC/MS) / Judy Peat [and others]
  • Development of an assay for methotrexate and Its metabolites 7-hydroxy methotrexate and DAMPA in serum by LC-MS/MS / Ryan C. Schofield [and others]
  • Quantitative, multidrug pain medication testing by liquid chromatography : tandem mass spectrometry (LC-MS/MS) / Geza S. Bodor
  • Quantification of free phenytoin by liquid chromatography tandem mass spectrometry (LC/MS/MS) / Judy Peat, Clint Frazee, and Uttam Garg
  • Detection of stimulants and narcotics by liquid chromatography-tandem mass spectrometry and gas chromatography-mass spectrometry for sports doping control / Brian D. Ahrens, Yulia Kucherova, and Anthony W. Butch
  • Quantification of tricyclic antidepressants in serum using liquid chromatography electrospray tandem mass spectrometry (HPLC-ESI-MS/MS) / Christopher A. Crutchfield, Autumn R. Breaud, and William A. Clarke.
This volume describes methods and protocols for a number of drugs and toxins in a stepwise manner. Chapters in the book cover a wide array of topics such as: quantitation of Flecainide, Mexiletine, Propafenone, and Amiodarone in Serum or Plasma; quantitation of total Buprenorphine and Norbuprenorphine in Meconium; quantitation or Carisoprodol and Meprobamate in Urine; and quantitation of Tricyclic Antidepressants in Serum. Each chapter contains a brief introduction to the topic, clinical utility of the analyte(s), and useful notes to help laboratorians easily reproduce the protocols discussed. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and thorough, Clinical Applications of Mass Spectrometry in Drug Analysis: Methods and Protocols, is a great resource for laboratorians who are already using mass spectrometry or thinking of introducing this technology to their laboratories.
(source: Nielsen Book Data)9781493932511 20160619
Biology Library (Falconer)
Book
1 online resource (9 p. ) : digital, PDF file.
Terpenoids, naturally occurring compounds derived from isoprene units present in pine oleoresin, are a valuable source of chemicals used in solvents, fragrances, flavors, and have shown potential use as a biofuel. This paper describes a method to extract and analyze the terpenoids present in loblolly pine saplings and pine lighter wood. Various extraction solvents were tested over different times and temperatures. Samples were analyzed by pyrolysis-molecular beam mass spectrometry before and after extractions to monitor the extraction efficiency. The pyrolysis studies indicated that the optimal extraction method used a 1:1 hexane/acetone solvent system at 22°C for 1 h. Extracts from the hexane/acetone experiments were analyzed using a low thermal mass modular accelerated column heater for fast-GC/FID analysis. The most abundant terpenoids from the pine samples were quantified, using standard curves, and included the monoterpenes, α- and β-pinene, camphene, and δ-carene. Sesquiterpenes analyzed included caryophyllene, humulene, and α-bisabolene. In conclusion, diterpenoid resin acids were quantified in derivatized extractions, including pimaric, isopimaric, levopimaric, palustric, dehydroabietic, abietic, and neoabietic acids.
Book
Article No. 11594 : digital, PDF file.
The growth of freshly formed aerosol particles can be the bottleneck in their survival to cloud condensation nuclei. It is therefore crucial to understand how particles grow in the atmosphere. Insufficient experimental data has impeded a profound understanding of nano-particle growth under atmospheric conditions. Here we study nano-particle growth in the CLOUD (Cosmics Leaving OUtdoors Droplets) chamber, starting from the formation of molecular clusters. We present measured growth rates at sub-3 nm sizes with different atmospherically relevant concentrations of sulphuric acid, water, ammonia and dimethylamine. We find that atmospheric ions and small acid-base clusters, which are not generally accounted for in the measurement of sulphuric acid vapour, can participate in the growth process, leading to enhanced growth rates. The availability of compounds capable of stabilizing sulphuric acid clusters governs the magnitude of these effects and thus the exact growth mechanism. Furthermore, we bring these observations into a coherent framework and discuss their significance in the atmosphere.
Book
xxiii, 350 pages, 46 unnumbered pages of plates : illustrations (some color) ; 25 cm
Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.
(source: Nielsen Book Data)9781118616499 20160704
Biology Library (Falconer)
Book
1 online resource (Article No. 026103 ) : digital, PDF file.
Empirical observations show that sodium(Na) is a benign contaminant in some thin-filmsolar cells. Here, we intentionally contaminate thermally evaporated tin sulfide (SnS)thin-films with sodium and measure the SnS absorber properties and solar cellcharacteristics. The carrier concentration increases from 2 × 10<sup>16</sup> cm<sup>-3</sup> to 4.3 × 10<sup>17</sup> cm<sup>-3</sup> in Na-doped SnSthin-films, when using a 13 nm NaCl seed layer, which is detrimental for SnS photovoltaic applications but could make Na-doped SnS an attractive candidate in thermoelectrics. We observed trends in carrier concentration and found that it is in good agreement with density functional theory calculations, which predict an acceptor-type NaSn defect with low formation energy.
Book
xii, 298 p. : ill. ; 25 cm
Introduction to Protein Mass Spectrometry provides a comprehensive overview of this increasingly important, yet complex, analytical technique. Unlike many other methods which automatically yield an absolutely unique protein name as output, protein mass spectrometry generally requires a deduction of protein identity from determination of peptide fragmentation products. This book enables readers to both understand, and appreciate, how determinations about protein identity from mass spectrometric data are made. Coverage begins with the technical basics, including preparations, instruments, and spectrometric analysis of peptides and proteins, before exploring applied use in biological applications, bioinformatics, database, and software resources. Citing the most recent and relevant work in the field of biological mass spectrometry, the book is written for researchers and scientists new to the field, but is also an ideal resource for those hoping to hone their analytical abilities. * Offers introductory information for scientists and researchers new to the field, as well as advanced insight into the critical assessment of computer-analyzed mass spectrometric results and their current limitations* Provides examples of commonly-used MS instruments from Bruker, Applied Biosystems, JEOL, Thermo Scientific/Thermo Fisher Scientific, IU, and Waters* Includes biological applications and exploration of analytical tools and databases for bioinformatics.
(source: Nielsen Book Data)9780128051238 20160619
Biology Library (Falconer)
Book
xxviii, 466 pages : illustrations ; 24 cm.
Covers the area of lipidomics from fundamentals and theory to applications * Presents a balanced discussion of the fundamentals, theory, experimental methods and applications of lipidomics * Covers different characterizations of lipids including Glycerophospholipids; Sphingolipids; Glycerolipids and Glycolipids; and Fatty Acids and Modified Fatty Acids * Includes a section on quantification of Lipids in Lipidomics such as sample preparation; factors affecting accurate quantification; and data processing and interpretation * Details applications of Lipidomics Tools including for Health and Disease; Plant Lipidomics; and Lipidomics on Cellular Membranes.
(source: Nielsen Book Data)9781118893128 20160704
Biology Library (Falconer)
Book
1 online resource ()
Mass Spectrometry: Techniques for the Structural Characterization of Glycans presents new methods for conducting detailed carbohydrate qualitative analysis-arming analytical chemists, pharmaceutical scientists, and food scientists with a quick reference that will allow them to determine the structures of carbohydrates molecules. As there is a need in the scientific community for content specific to structural determination and analysis of new glycoprotein drug, and because structure-activity analysis requires a structural determination of the N- and O-linked oligosaccharides linked to glycol-proteins, this book provides the relevant research that are necessary for advances and new outcomes in this area of study.
Book
Article No. e0154043 : digital, PDF file.
<i>Methylobacterium extorquens</i> AM1 is a facultative methylotroph capable of growth on both single-carbon and multi-carbon compounds. The ethylmalonyl-CoA (EMC) pathway is one of the central assimilatory pathways in <i>M. extorquens</i> during growth on C1 and C2 substrates. Previous studies had shown that ethylmalonyl-CoA mutase functioned as a control point during the transition from growth on succinate to growth on ethylamine. In this study we overexpressed <i>ecm</i>, <i>phaA</i>, <i>mcmAB</i> and found that upregulating ecm by expressing it from the strong constitutive <i>mxaF</i> promoter caused a 27% decrease in growth rate on methanol compared to the strain with an empty vector. Targeted metabolomics demonstrated that most of the central intermediates in the <i>ecm</i> over-expressing strain did not change significantly compared to the control strain; However, poly-β-hydroxybutyrate (PHB) was 4.5-fold lower and 3-hydroxybutyryl-CoA was 1.6-fold higher. Moreover, glyoxylate, a toxic and highly regulated essential intermediate, was determined to be 2.6-fold higher when <i>ecm</i> was overexpressed. These results demonstrated that overexpressing ecm can manipulate carbon flux through the EMC pathway and divert it from the carbon and energy storage product PHB, leading to an accumulation of glyoxylate. Furthermore, untargeted metabolomics discovered two unusual metabolites, alanine (Ala)-meso-diaminopimelic acid (mDAP) and Ala-mDAP-Ala, each over 45-fold higher in the <i>ecm</i> overexpressing strain. These two peptides were also found to be highly produced in a dose-dependent manner when glyoxylate was added to the control strain. Overall, this work has explained a direct association of <i>ecm</i> overexpression with glyoxylate accumulation up to a toxic level, which inhibits cell growth on methanol. Lastly, this research provides useful insight for manipulating the EMC pathway for efficiently producing high-value chemicals in <i>M. extorquens</i>.
Book
1 online resource (18 p. ) : digital, PDF file.
The ARABIDOPSIS SKP1-LIKE1 (ASK1) protein functions as a subunit of SKP1-CUL1-F-box (SCF) E3 ubiquitin ligases. Previous genetic studies showed that ASK1 plays important roles in Arabidopsis flower development and male meiosis. However, the molecular impact of ASK1-containing SCF E3 ubiquitin ligases (ASK1-E3s) on the floral proteome and transcriptome is unknown. Here we identified proteins that are potentially regulated by ASK1-E3s by comparing floral bud proteomes of wild-type and the ask1 mutant plants. More than 200 proteins were detected in the ask1 mutant but not in wild-type and >300 were detected at higher levels in the ask1 mutant than in wild-type, but their RNA levels were not significantly different between wild-type and ask1 floral buds as shown by transcriptomics analysis, suggesting that they are likely regulated at the protein level by ASK1-E3s. Integrated analyses of floral proteomics and transcriptomics of ask1 and wild-type uncovered several potential aspects of ASK1-E3 functions, including regulation of transcription regulators, kinases, peptidases, and ribosomal proteins, with implications on possible mechanisms of ASK1-E3 functions in floral development. In conclusion, our results suggested that ASK1-E3s play important roles in Arabidopsis protein degradation during flower development. This study opens up new possibilities for further functional studies of these candidate E3 substrates.
Book
xiii, 306 pages : illustrations (some color) ; 26 cm.
  • Increased depth and breadth of plasma protein quantitation via two-dimensional liquid chromatography/multiple reaction monitoring-mass spectrometry with labeled peptide standards / Andrew J. Percy ... [et al.]
  • Quantitative analysis of the Sirt5-regulated lysine succinylation proteome in mammalian cells / Yue Chen
  • Determining the composition and stability of protein complexes using an integrated label-free and stable isotope labeling strategy / Todd M. Greco, Amanda J. Guise, and Ileana M. Cristea
  • Label-free quantitation for clinical proteomics / Robert Moulder, Young Ah Goo, and David R. Goodlett
  • Proteogenomic methods to improve genome annotation / Keshava K. Datta, Anil K. Madugundu, and Harsha Gowda
  • Mass spectrometry-based quantitative O-GlcNAcomic analysis / Junfeng Ma and Gerald W. Hart
  • Isolating and quantifying plasma HDL proteins by sequential density gradient ultracentrifugation and targeted proteomics / Clark M. Henderson, Tomas Vaisar, and Andrew N. Hoofnagle
  • Method for label-free, differential top-down proteomics / Ioanna Ntai ... [et al.]
  • Multiplexed immunoaffinity enrichment of peptides with anti-peptide antibodies and quantification by stable isotope dilution multiple reaction monitoring mass spectrometry / Eric Kuhn and Steven A. Carr
  • High-throughput quantitative proteomics enabled by mass defect-based 12-plex DiLeu isobaric tags / Dustin C. Frost and Lingjun Li
  • Isotopic N, N-Dimethyl leucine (iDiLeu) for absolute quantification of peptides using a standard curve approach / Tyler Greer and Lingjun Li
  • Selecting optimal peptides for targeted proteomic experiments in human plasma using in vitro synthesized proteins as analytical standards / James G. Bollinger ... [et al.]
  • Using the CPTAC assay portal to identify and implement highly characterized targeted proteomics assays / Jeffrey R. Whiteaker ... [et al.]
  • Large-scale and deep quantitative proteome profiling using isobaric labeling coupled with two-dimensional LC-MS/MS / Marina A. Gritsenko ... [et al.]
  • Multiple and selective reaction monitoring using triple quadrupole mass spectrometer : preclinical large cohort analysis / Qin Fu ... [et al.]
  • Methods for SWATH™ : data independent acquisition on tripleTOF mass spectrometers / Ronald J. Holewinski ... [et al.]
  • Measurement of phosphorylated peptides with absolute quantification / Raven J. Reddy ... [et al.]
  • Proteomic analysis of protein turnover by metabolic whole rodent pulse-chase isotopic labeling and shotgun mass spectrometry analysis / Jeffrey N. Savas, Sung Kyu Park, and John R. Yates, III.
This volume describes prominent methodologies developed by laboratories that have been leading the field of quantitative proteomics by mass spectrometry. The procedures for performing the experiments are described in an easy-to-understand manner with many technical details that usually are not reported in typical research articles. This second edition of Quantitative Proteomics by Mass Spectrometry provides a broad perspective of the methodologies used for quantifying proteins and post-translational modifications in different types of biomedical specimens. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and thorough, Quantitative Proteomics by Mass Spectrometry, Second Edition is a valuable resource to help researchers understand and learn about the latest tools used in the study of quantitative proteomics by mass spectrometry.
(source: Nielsen Book Data)9781493935222 20160704
Biology Library (Falconer)
Book
05/10/2016 : digital, PDF file.
Photosystem II (PSII) is a photosynthetic membrane-protein complex that undergoes an intricate, tightly regulated cycle of assembly, damage, and repair. The available crystal structures of cyanobacterial PSII are an essential foundation for understanding PSII function, but nonetheless provide a snapshot only of the active complex. To study aspects of the entire PSII life-cycle, mass spectrometry (MS) has emerged as a powerful tool that can be used in conjunction with biochemical techniques. In this article, we present the MS-based approaches that are used to study PSII composition, dynamics, and structure, and review the information about the PSII life-cycle that has been gained by these methods. This information includes the composition of PSII subcomplexes, discovery of accessory PSII proteins, identification of post-translational modifications and quantification of their changes under various conditions, determination of the binding site of proteins not observed in PSII crystal structures, conformational changes that underlie PSII functions, and identification of water and oxygen channels within PSII. Lastly, we conclude with an outlook for the opportunity of future MS contributions to PSII research.
Book
1 online resource (xviii, 176 pages) : illustrations (some color).

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