Proteomics Today discusses the increasingly important role of mass spectrometry in proteomic research, and emphasizes recent advances in the existing technology and describes the advantages and pitfalls as well.
- Provides a scientifically valid method for analyzing the approximatey 500,000 proteins that are encoded in the human genome
- Explains the hows and whys of using mass spectrometry in proteomic analysis
- Brings together the latest approaches combining separation techniques and mass spectrometry and their application in proteome analysis
- Comments on future challenges and how they may be addressed
- Includes sections on troubleshooting
Contents
Instrumentation and Developments
- Ionization Techniques for Macromolecules
- Examples on Analytical Solutions Based on FAB–MS
- Electrospray Ionization
- Matrix-Assisted Laser Desorption Ionization
- Ion Detection
- Types of Analyzers
- Hybrid Analyzers
- Tandem Mass Spectrometry
- Current MS Instrumentation in Proteome Analyses
- Current MS-Based Proteomics
Proteomics in Cancer Research
- Pancreatic Ductal Adenocarcinoma
- Proteomic Analysis of Human Breast Carcinoma
- Proteomic Profiling of Chemoresistant Cancer Cells
- Signal Pathway Profiling of Prostate Cancer
- Emerging Role of Functional and Activity-Based Proteomics in Disease Understanding
- Activity-Based Protein Profiling
- Probing Protein Functions Using Chromophore-Assisted Laser Inactivation
- Role of Protein–Tyrosine Kinases
Current Strategies for Protein Quantification
- Global Internal Standard Technology
- Differential In-Gel Electrophoresis
- Quantification of Modified Proteins
- Comments and Considerations
- Other Approaches
- Emerging Role of Microfluidic Devices
Convential Isoelectric Focusing in Gel Matrices and Capillaries and Immobilized pH Gradients
- Conventional Isoelectric Focusing in Amphoteric Buffers
- Immobilized pH Gradients
- Capillary Isoelectric Focusing
- Separation of Peptides and Proteins by CZE in Isoelectric Buffers
Sodium Dodecyl Sulfate—Polyacrylamide Gel Electrophoresis
- SDS–Protein Complexes: a Refinement of the Model
- Theoretical Background of Mr Measurement by SDS–PAGE
- Methodology
- Gel Casting and Buffer Systems
- Blotting Procedures
Two-Dimensional Maps
- Some Basic Methodology Pertaining to 2D PAGE
- Prefractionation Tools in Proteome Analysis
- Multidimensional Chromatography Coupled to MS
- Protein Chips and Microarrays
- Nondenaturing Protein Maps
- Spot Matching in 2D Gels via Commercial Software
Index