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Book Review Coincidence Tables for Atomic Spectroscopy. By J. Kuba L. Kucera F. Plzk M. Dvoak and J

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the standard handbook of every protein chemist. Now, ten
years later, the first volumes of the second edition have been
published. Owing to the illness and untimely death of the
co-editor of the first edition, K . Bailey, the second edition is
edited by Neurath alone.
The second edition, like the first, is to comprise four volumes.
However, it is not a new edition in the true sense, but a
completely new version oriented along different lines. This
is evident from the subtitle: “Composition, Structure, and
Function”, and from the fact that only three of the contributors to the first edition have also contributed to the
second. The principal theme of the work is no longer the
question of the chemical structure of the proteins, but the
problem of the relationship between the structure of a protein
and its specific biological function. Comparison of the new
edition with the old will make clear the progress that has
been made in this field of biochemistry.
The first chapter of Volume I1 deals with the conformation
of the polypeptide chains of proteins in solution (J. A . Schellman and C . Schellman), while the last chapter is concerned
with the X-ray structure analysis of proteins (Dickerson);
these two chapters are closely related, and even overlap in
part. The general theoretical principles and the experimental
methods used in the determination of the structures of
proteins are described in detail, and the facts noted are
discussed. Dickerson gives a list of the proteins that are
under investigation by X-ray analysis.
The chapters by Steinhardt and Beychok, “Interaction of
Proteins with Hydrogen Ions and Other Small Ions and
Molecules,” and by Nichol, Bethune, Kegeles, and Hess,
“Interacting Protein Systems,” are devoted to the interactions of proteins with proteins or components of low
molecular weight. The first of these two chapters is mainly
concerned with the acid-base equilibria of proteins, and so
provides a basis for the discussion of the pH-dependence of
various protein functions. The chapter on protein-protein
interactions has a pronounced physico-chemical bias. This
chapter is very informative o n the subject of the quaternary
structure of many proteins and on the problem of the antigenantibody reaction. A particularly impressive chapter is
“Polyamino Acids as Protein Models” by Katchalski, Seln,
Silman, and Berger, which describes the synthesis and the
chemical, physico-chemical, and biological properties of
polypeptides, and deals with all the results published in this
field. It becomes clear from this chapter how much the
elucidation of the structure of proteins, of the genetic code,
and of immunological problems owes to studies on synthetic
polypeptides.
The first and last chapters of Volume 111 are of a general
nature, while the other four chapters deal with the structures
and functions of various proteins. Sober, Hartley, Carroll,
and Peterson give a very instructive treatment of the “Fractionation of Proteins” (solubility, chromatography, electrophoresis, sedimentation, dialysis, ultrafiltration, and immunological methods), and also describe the methods used for
the characterization of proteins and the determination of
their purity. Weber and Teale (“Interaction of Proteins with
Radiation”) discuss the infrared and ultraviolet spectroscopy,
fluorescence, light scattering, and optical rotatory dispersion of
proteins Fraenkel-Conrat gives a brief outline of the structures and functions of virus proteins, and Putnam (“Structure and Function of the Plasma Proteins”) and Singer (“Structure and Function of Antigen and Antibody Proteins”)
presents a lucid, impressive survey of the plasma proteins
and the antigen-antibody proteins. Finally, Davie and Ratnoflgive a clear description of the various factors that effect
the coagulation of blood.
The various chapters are well written by competent authors,
and special emphasis is laid throughout on the description
of the experimental methods. The literature covered includes
very recent publications, so that we are shown the latest
situation in each field. These reports are indispensable to
anyone who is concerned with proteins. There is only one
objection to this work: one gains the impression that the
328
arrangement of the chapters is arbitrary ( e . g . chapters 7, 11
and 17 would be expected to appear together in that order).
This gives the volumes a certain “Advances” character.
Regrettable omissions include a somewhat more detailed
treatment of denaturation and a chapter on the size and
shape of protein molecules such as that contributed by Edsall in the 1st Edition (which will consequently still have to
be consulted as before). Only a few misprints were found,
and the print and layout, with the exception of the cover, are
good.
H . Sund
[NB 441,’276 IE]
Coincidence Tables for Atomic Spectroscopy. By J. Kuba,
L. KuCera, F. Plzcik, M. Dvofak, and J. Mrdz. Elsevier
Publishing Comp., Amsterdam-London-New York 1965.
1st Edit., XXXI + 1136 pp., about $ 18.00
Anyone who is concerned with trace analysis by emission
spectroscopy must constantly ask himself what foreign
elements could interfere with a detection or even make it
doubtful. Kuba and his co-workers have now used all the
published data to produce a comprehensive book of tables
(about 1150 pages) that supplies the answer to this question
immediately.
The emission lines of 90 elements (only At, Bk, Cf, Es, Fm,
Fr, Md, No, Pm, Po, and Tc are excluded) between 2000 and
10000 8, are presented in 17 tables. Table IV and V give
lines that can be used for the analysis of the rare earths,
Table VI for a number of actinides, and Tables VII and VIII
for gases. Table IX gives the spark spectrum of air, and
calibration lines for the secondary standard Fe are given to
at least three decimal places in Tables X and XI. Tables XI1
and XI11 contain the emission lines of inorganic molecules
and fragments (e.g. A10, BeO, Cz, CN, and CaF). Finally,
Table XIV gives the ionization energies of the elements and
of their ions.
The principal tables - Table XVI for 73 elements, with a
total of 683 analytically important lines ( e . g . resonance
lines), and Table XVII for the rare earths - cover 1050 pages,
the elements being arranged alphabetically and in order of
increasing wavelength of the most important lines. All
interfering emission lines there are always a few dozen!)
due to foreign elements are also listed on the following basis:
the entire coincidence region is assumed to be so wide that
the resolution of two lines on a photographic plate must be
possible; the coincident lines are then noted according to
their relative intensities for three ranges 5 Ah. To save
unnecessary searching on the part of analysts with highresolution equipment, the coincident lines are given in three
types of print bold, normal, and italic (corresponding to
linear dispersions of 0.5 to 5 , 2 to 30, and > 30 8,/mm).
A very disturbing fault is the fact that the tables contain
practically no legends or explanations for the symbols used,
so that the explanations must be sought in the text in the
very early part of the book. Thus in Table I (p. XVII)
reference should be made to Table XVI (p. 95), and the
explanation of the table “Dislocation of Main Lines” (pp.
63-91) is given o n p. XVIII. The values given in Tables X
and XI for the standard Fe d o not agreeexactly; no indication
of the source of Table X is given. According to the text on
p. XVI, Table XI should contain calibration lines for the
standards Cd, Kr, and Fe, whereas according to p. 52 these
lines refer only to Fe.
On the whole, this is an excellent and important bqok in a
very good and hard-wearing form - a book for the practical
[NB 442/277 IE1
analyst.
W . Jung
Coordination Chemistry. By F. Bas010 and R. C . Johnson.
W. A. Benjamin, Inc., New York-Amsterdam 1964. 1st
Edit., XI1 + 180 pp., numerous illustrs. and several tables,
linen, $ 4.35.
This book is intended as an introduction to coordination
chemistry for American chemistry students. A very skilful
treatment of molecular orbital methods and ligand field
Angew. Chem. internat. Edit.
VoI. 5 (1966) 1 No. 3
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