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PROTEINS: Structure, Function, and Genetics 28:140 (1997)
BOOK REVIEW
Protein Methods, 2nd edit., by Daniel M.
Bollag, Michael D. Rozycki, and Stuart J.
Edelstein. New York: Wiley-Liss, Inc.
This 415-page book covers 12 aspects of protein
methods in the following order: 1) preparation for
protein isolation; 2) protein extraction and solubilization; 3) protein concentration determination; 4) concentrating protein solutions; 5) gel electrophoresis
under denaturing conditions; 6) gel electrophoresis
under nondenaturing conditions; 7) isoelectric focusing and two-dimensional gel electrophoresis; 8) immunoblotting; 9) ion exchange chromatography; 10)
gel filtration chromatography; 11) affinity chromatography; and 12) hanging drop crystallization. In this
respect the book is quite thorough.
This book is a gold mine for new graduate students
commencing a protein project for the first time. In
fact, this reviewer gave the book to a new rotation
student who fell in love with it and used it extensively during his 3 month rotation project. It is also a
gold mine for new faculty members who spent their
graduate career studying cell biology or genetics and
now realize they want to bring their work to a
r 1997 WILEY-LISS, INC.
molecular level of understanding. In very clear, step
by step language the book explains how to work with
proteins. It will be particularly useful to many
investigators who are overexpressing proteins in E.
coli and wish either to obtain their protein from
inclusion bodies or to avoid inclusion bodies altogether. The chapter on protein crystallization will be
particularly helpful in getting new investigators
started in protein crystallography.
Some may find the book is lacking in two respects.
Details on how to work with membrane proteins are
not emphasized, although there are places throughout where some discussion of this topic occurs. Also,
there are no chapters focused on the sedimentation
of proteins.
In summary, this is an excellent Protein Methods
book that every Ph.D. advisor should buy as a gift for
students in their laboratory engaged in protein
work.
Pete Pedersen
Department of Biological Chemistry
Johns Hopkins University
Baltimore, MD
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