APRIL, 19%
221
system of qualitative analysis based on the traditional sulfide method using semimicro quantities. Brief reports of data and answers to pertinent questions arc facilitated by perforation of the pages. Included in the appendix are lists of apparatus and supplies needed.
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EWERIMENTS AND PROBLEMS FOR COLLEGE CHEMISTRY
1. E. Belcher and I. C. Colbert, University of Oklahoma. Fifth edition. Appleton-Century-Crofts, Inc., New York, 1953. x 214 pp. 25 figs. 21.5 X 28 cm. $2.50.
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PROPUlTlES AND NUMERICAL RELATIONSHIPS OF THE COMMON ELEMENTS AND COMPOUNDS
I. E. Belcher and I. C. Colbert, University of Oklahoma. Fifth edition. Appleton-Century-Crofts, Inc., New York, 1953. x 42 figs. 21.5 X 28 em. $3.
374 pp.
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BOTHmanual8 are e8peciaIIy adapted to use with the SmithEhret texts and have page references to them, but are easily adapted for use with other texts. Parts I, 11, and 111 of both manuals are identical. Part I consists of 39 experiments, Part I1 is an outline of work in first-year chcmist~ywith references to the Smith texts, and Part I11 is a textbook of chemical arithmetic with lists of problems. Experiments are fairly simple, of traditional type, with complete discussion and directions, and with very detailed and complete reports. Report sheets are perforated to hand in and two blanks for each report are provided so that a carbon copy can he kept by the student. However, the authors themselves point out that this method focuses attention on report writing and encourages copying so do not recommend it. No qualitative analysis is included in this ms,nual. The appendixes include tables of vapor pressures, atomic weights, logarithms, lists of materials and apparatus required, and indicat,ors. In addition to the above common material, the "Properties and Numsrical Relationships'' manual has Part IV, Properties of the Common Elements and Related Compounds, a series of 28 additional experiments similar in nature to those described under Part I, and Part V, Elementary Qualitative Analysis, which is s misleading title in that no systemtic qualitative analysis is included. Instead, this is a group of five experiments on amphoteric ~ubstitnces, colloids, solubility product,, complex ions, and electromotive-force scrica. FRED C. FREYTAG
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NATURE AND STRUCTURE OF COLLAGEN
Edited by I. T. Randall, Honorary Director, Medical Research Council Biophysics Research Unit, and Wheatstone Professor of Physics, University of London, and Sylvia Fitton Jackson. 269 pp. Many figs. Academic Press Inc., New York, 1953. ix Tables. 14.5 X 22 em. $6.50.
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THISis a group of papers presented far a. discussion convened hy the Colloid and BiophysiesCommittee of the Fsrsday Society, in 1953. Chief object of the meetings was to bring together as many of the interested research workers as possible for discussion of the varied biological, physical, and biochemical problems. Approximately 100 people attended the sessions. The 23 pspers included farm a mosaic of relatively disconnected subjects, though contrihuting materially to the literature on connective tissues. The papers were interspersed with nine discussion periods bringing out rriuch pertinent information and clarification. The subjects covered in this symposium can he divided into eight natural groups and will be dealt with in what seems like a logical sequence
without regard to the order of appearance of the papers in the book. Three papers are devoted to the origin of collagen under the titles "Metabolism of collagen in the rat," "Fibrogenesia in vivo and in vitro," and "The physical and chemical properties of fibre formation and structure." Three other papers cover the properties of specific materink, retieulin,. byssus threads, and dentine . collagen. Physical properties such as X-ray crystallographic studies, high-angle X-ray diffraction, infrared absmption, seattming of light by collagen solutions, quantitative paper chromatography, the electrophoresis of eolhgen solutions, and Dannan membrane equilibrium are discussed in seven papers. Two papers are devoted to chemical observations on camposition of human subcutaneous tissue and on extracted collagens. The remaining three group? of pspers deal with enzyme studies, three papers; the reconstruction of collagen fibrils, one paper; and there is one paper devoted to the physical and chemical properties of extracted skin collagen. This hook is certainly not designed for the casual reader but has value only for the specialist in the field. From his point of view, i t represents a. valuable addition to the literatuture on eonnective tissue. On reding the book, one is impressed by the number of uncertainties and unsolved problems concerning a substance that certainly must be regarded as one of the simpler tissues in living organisms. He is also imuressed bv the stuuondous amount i f work that is represent,ed' by a modest advance it) knowledge in such a. field.
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THE CHEMICAL STRUCTURE OF PROTEINS
Edited by G. E. W.Wolstenholme and Margaret P. Cameron. Little. Brawn and Co., Boston, 1954. xii 222 pp. 49 figs. Tables. 14 X 21 cm. $6.
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SINCE1949 the Ciba Foundation in London hss held over two dozen international symposia dealing with selected fields of medical and chemical research. The invited papers, together with inform1 discussions which follow them, itre published in hook form. "The Chemical Structure of Proteins" is a report on the meetings held in December, 1952. The papers deal with three main topics: the isolation of pure proteins and peptides, the characterization of end groups, and the splitting of specific peptidc bonds. Countorcurrent distribution methods as appiied to the elueidatian of the structure of tyroeidine A are discussed by L. C. Craig; the purification of ribonuelease and lysozyme with ion-exchange IV. L. Stein: and the oartition chromachramatoereohv hv " tography of insulin and glucagan'hy It. R. Porter. These are three excellent examples of the diversificstion of techniques used for isolating pure moleoular species. R. L. M. Synge considers the peptides of ordinary tissue and discusses their role in protein synthesis and the effect of their adsorption on the apparent composition of proteins. Various techniques of end-group analysis are considered. P. Desneuelle and M. Rovery use the Sanger D F P method to study the N-terminal groups of trypsinogen, trypsin, chymotrypsinogen, and chymotrypsin. P. E d m m discusses his newer phenylisothiocyannte method for N-terminal residue analysis, and H. FmenkelConrat desoribes its use a n a variety of proteins. The identification of carboxyl terminal residues by reduction to amino alcohols is considered in two papers by A. C. Chihnall and M. W. Rees, and C. Fromsgeot and M. Justiea. Rercntly developed techniques for degrading peptides from the amino and esrboxyl ends are described by F. Turba and T. Wieland. These papers well illustrate the variety of chemical methods which are being erdored hv manv different erouns. The import:lnt proldrm of zclrotivr rle.rwgr. of amino-will r l e h . Ily 1,rin~inl:rhout ;tvyl n~igrnlion?from x ~ n i r l oto nvighbol7
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