Principles and Practice of Biological Mass Spectrometry Chhabil Dass Wiley-Interscience, 416 pp, hardcover, 2001

This book would be an invaluable starting point for someone interested in becoming familiar with mass spectrometry, or for chemists or biochemists who wish to obtain a broad overview of protein MS. The advantages and disadvantages of each type of spectrometer are clearly discussed, and the author tries to give an unbiased appraisal; however, he is clearly more familiar with ESI and MALDI than other types, such as magnetic sector or FT-ICR MS. There are few details on interpreting mass spectra, and no detailed protocols; the book concentrates on its task of painting the broad outlines of its subject, which it does very well.

However, the writing style is a bit dull, contains many careless mistakes and typos, and is confusing in places. For example, on page 249 the author says that fast atom bombardment (FAB) MS is practically useless for glycoproteins because glycopeptides rarely give a signal; but 5 pages later, after a detour through ESI and MALDI, the author returns to FAB and says that it is customary to derivatize glycopeptides before FAB-MS, and that FAB-MS analysis of glycoproteins provides a wealth of information, including compositions, heterogeneity, and oligosaccharide sequences. Figure 9.1, which illustrates the principal ion fragmentation patterns of peptides, is hopelessly screwed up, and the book contains a number of awkward sentences that require prior knowledge before their meaning can be disambiguated. Despite the many points of comparison of the different types of mass spectrometry throughout the book, it is not until page 289 that the author gets around to saying that MALDI is at least 10 times more sensitive than ESI. Nonetheless, the book is highly recommended to anyone interested in understanding mass spectrometers.

Here are two sample paragraphs, one from each of the two sections:

A PAD [postacceleration detector]-based detector used in Micromass (Beverly, MA) instruments contains two conversion dynodes, one for positive ions and one for negative ions, a phosphor, and a photomultiplier (Figure 3.15). For positive-ion detection, the conversion dynode is maintained at -10 to -20 kV, and the emitted secondary electrons are accelerated toward the phosphor-coated electrode, the voltage of which is varied between 10 and 20 kV. When operated for the detection of negative ions, the incoming beam is first deflected toward a cylinder-shaped conversion dynode held at half the phosphor voltage. The positive charge on the phosphor attracts the emitted electrons toward it.

The precursor ion scan of specific marker ions (e.g., m/z 204) is another viable means of selective detection of glycopeptides[26]. For example, the MS2 of a tandem instrument can be set to monitor m/z 204, and the MS1 is scanned to detect those glycopeptides that fragment to yield the m/z 204 oxonium ion. This technique provides improved selectivity, but is less sensitive than the stepped-orifice voltage-scanning procedure.

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