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by physical chemistry and clays, made easy by the absence of destructive life itself. The actual mechanisms proposed are rational and individually possible, but the whole conveys a lack of conviction, which the author is plainly ready to concede. It is as though atomic physicists sought to explain chemistry in the days before the discovery of the Pauli principle. The comments by N. W. Pirie are shrewd and add a great deal to the book. E. C. POLLARD,New Haven, Connecticut Physiologische Chemie. Ein Lehr- und Handbuch fuer Aerate, Biologen und Chemiker. Hervorgegangen aus dem Lehrbuch der Physiologischen Chemie von OLOFHAMMARSTEN. Erster Band : Die Stoffe. Herausgegeben von B. FLASCHENTRAEGER unter Mitwirkung von E. LEHNARTZ.Springer Verlag, Berlin, Goettingen and Heidelberg, 1951. viii f 1600 pp. Price DM 198. This is a completely revised edition of the well-known text by 0. Hammarsten. On its original publication in 1890, the book was intended to serve advanced students and medical doctors as a short, condensed, and disinterested presentation of the results of research in the field of physiological chemistry as well aa to record its methods. Eleven editions of this famous text were published in the course of 36 years. In 1936 the plan for a thorough revision was conceived. Due to the fact that the field has expanded to an unexpected extent, it was felt that the text should serve not only the medical profession but mainly the biologist and the broadminded chemist, Dr. Flaschentraeger who transferred his activities from Ziirich to Alexandria, Egypt, after the war, ,undertook the great and commendable task of preparing the new edition. Individual chapters were contributed by D. Ackermann, G. Blix, H. Bredereok, P. Brigl, A. Butenandt, K. Felix, B. Flaachentraeger, F. Flury, K. Freudenberg, K. Gemeinhardt, W. Grassmann, Chr. Grundmann, F. Holtz, E. Klenk, F. Knoop, H. Kraut, W. Kuhn, H. Mueller, Th. Ploete, F. Schneider, G. Schramm, W. Siedel, T. Thunberg, J. Trupke, R. Weidenhagen, A. Weischer and K. Zeile. The tremendous strides made in the elucidation of the structure of biologically important substances as well as our increasing knowledge of the mechanism of biochemical reactions and their interrelationsh:p required that the material be divided into two volumes according to the classical system. The present volume discusses the substrates while the one to follow is expected to deal with the dynamics of biochemical processes. The volume under review contains an astonishingly thorough and comprehensive description, in 16 chapters, of the physicochemioal foundations of biological processes as well as inorganic and organic substances such as salts, carbohydrates, fats and lipides, proteins, purines, pyrimidines, pigments, enzymes, and animal poisons. The name and subject index alone covers 343 pages, giving a clear-cut indication of the immense scope of the material. Following the present trend in biochemistry, the chapter 09 enzymes alone covers 265 pages. The entire volume as such attests to extremely thorough documentation. It was difficult to discover significant or disturbing misprintrr. A11 in all, this “text” represents a revival of the excellent treatises which have always been a specialty of the prewar German school. Some of the references reach right up to the year
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1951. The book was printed by H. Stuere, Inc., in Wuerzburg, the printers of Beilstein’s Handbuch, which fact in itself is a guarantee of excellence in production. It is to be hoped that the second volume, the publication of which is tentatively promised for the autumn of 1952, will not be delayed. On its appearance and together with the present volume, biochemical research will possess a monumental and up-to-date cross section. The editor and the contributors are to be felicitated on the successful complet,ion of this task of Sisyphus. F. F. NORD, New York, New York
Addendum
to “MOLECULAR KINETICS OF MYOSIN ADENOSINE TRIPHOSPHATASE”
by L. Ouellet, K. J. Laidler, and M. F. Morales, Arch. Biochem. & Biophys. 39, 37 (1952). In specifying the purity of the ATP and myosin preparations used in the title paper we remarked that after chromatographic purification of the ATP the myosin action produced about .92 moles of orthophosphate for every mole of adenine ring (estimated by ultraviolet absorption at 260 mp), and we attributed the discrepancy of .08 moles to a presumably inert impurity remaining in the ATP. These considerations assumed the extinction coefficient of ATP to be 1.42 X 104, which was incorrect, since our measurements were made at pH 7.0 rather than pH 2. Using the correct value, 1.60 X 104, we conclude that the system produced very nearly 1 mole of orthophosphate per mole of adenine. In other words, the ATP was quite pure, and the myosin preparation had no myokinase activity.