Book contents
- Frontmatter
- Contents
- Preface to the seventh edition
- List of contributors
- List of abbreviations
- 1 Basic principles
- 2 Cell culture techniques
- 3 Centrifugation
- 4 Microscopy
- 5 Molecular biology, bioinformatics and basic techniques
- 6 Recombinant DNA and genetic analysis
- 7 Immunochemical techniques
- 8 Protein structure, purification, characterisation and function analysis
- 9 Mass spectrometric techniques
- 10 Electrophoretic techniques
- 11 Chromatographic techniques
- 12 Spectroscopic techniques: I Spectrophotometric techniques
- 13 Spectroscopic techniques: II Structure and interactions
- 14 Radioisotope techniques
- 15 Enzymes
- 16 Principles of clinical biochemistry
- 17 Cell membrane receptors and cell signalling
- 18 Drug discovery and development
- Index
- Plate section
- References
9 - Mass spectrometric techniques
- Frontmatter
- Contents
- Preface to the seventh edition
- List of contributors
- List of abbreviations
- 1 Basic principles
- 2 Cell culture techniques
- 3 Centrifugation
- 4 Microscopy
- 5 Molecular biology, bioinformatics and basic techniques
- 6 Recombinant DNA and genetic analysis
- 7 Immunochemical techniques
- 8 Protein structure, purification, characterisation and function analysis
- 9 Mass spectrometric techniques
- 10 Electrophoretic techniques
- 11 Chromatographic techniques
- 12 Spectroscopic techniques: I Spectrophotometric techniques
- 13 Spectroscopic techniques: II Structure and interactions
- 14 Radioisotope techniques
- 15 Enzymes
- 16 Principles of clinical biochemistry
- 17 Cell membrane receptors and cell signalling
- 18 Drug discovery and development
- Index
- Plate section
- References
Summary
INTRODUCTION
General
Mass spectrometry (MS) is an extremely valuable analytical technique in which the molecules in a test sample are converted to gaseous ions that are subsequently separated in a mass spectrometer according to their mass-to-charge (m/z) ratio and detected. The mass spectrum is a plot of the (relative) abundance of the ions at each m/z ratio. Note that it is the mass to charge ratios of ions (m/z) and not the actual mass that is measured. If for example, a biomolecule is ionised by the addition of one or more protons (H+ ions) the instrument measures the m/z after addition of 1 Da for each proton if the instrument is measuring positive ions or m/z minus 1 Da for each proton lost if measuring negative ions.
The development of two ionisation techniques, electrospray (ESI) and matrix-assisted laser desorption/ionisation (MALDI), has enabled the accurate mass determination of high-molecular-mass compounds as well as low-molecular-mass molecules and has revolutionised the applicability of mass spectrometry to almost any biological molecule. Applications include the new science of proteomics as well as in drug discovery. The latter includes combinatorial chemistry where a large number of similar molecules (combinatorial libraries) are produced and analysed to find the most effective compounds from a group of related organic chemicals.
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- Information
- Principles and Techniques of Biochemistry and Molecular Biology , pp. 352 - 398Publisher: Cambridge University PressPrint publication year: 2010