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Book Reviews Amino Aciris and Proteins. Cou S@itmroHARBORSmi POSIA ON QUANTITATIVE BIowoY, York: The Biological Laboratory, bor, 1950. Pp. 217. $7.00. Vol. 14. the x-ray datathat have been obtained on very large pro teins as well as smaller proteins and peptides, with a New Cold Spring Har stimulating discussion of the structural interpretations. Under the title “SizeRelationship among Similar Pro The selection of Amino Acids and Proteins as the topic for the fourteenth Cold Spring Harbor Symposium reflects the rapid progress that has been made in this field since the sixth (1988) symposium which dealt with ‘Protein Chemistry.― It is the only subject to which a second Cold Spring Harbor Symposium has been devot ed. This position aptly emphasizes the major role that the proteins play in biology. The fourteenth volume of this excellent series main tains the high standard of quality established by its predecessors. In the foreword it is mentioned that it was anticipated that there would be some duplication of the sixth symposium, lapping. but the reviewer has found There are 22 papers presented of the 88 authors, possible to review it seems desirable The first paper little over in VoL 14, and only S had papers in Vol. 6. It is im all the articles adequately; however, to mention names and general titles. by H. B. Bull deals with the molecu lan weight distribution of peptides in protein hydroly zates. J. R. Cairn and J. G. KirkWOOddiscuss results oh tamed in their application for “TheFractionation Convection.― rating amino of a new promising technic of Proteins by Electrophoresis distribution is described by L. C. Craig, J. D. Gregory, and G. T. Barry. Nearly one-third of the papers deal with some aspect of the amino acid composition of pro teins. W. H. Stein and S. Moore present data on the Composition Determination of the Amino Acid of Proteins.― Two papers deal with appli cations of the isotopic derivative technic to the analysis of proteins. The first, by A. S. Keston and S. Unden friend, discusses its general application, and the second, by M. Levy and E. Slobodiansky, describes on the Struc on “Structure and Enzymatic L. R. M. Synge reviews Break his own and other work and Some Implications for the Study may vary Two papers deal with the cytochemistry of proteins. J. F. Danielli describes the use of chromogenic reagents along with specific blocking reagents, and B. P. Kauf man, H. Gay, and M. R. McDonald describe the use of enzymes for the localization of cellular proteins. Two papers by S. Emerson and D. Shemin aspects of the biosynthesis deal with different of amino acids. “TheMetab olism of Peptides―is discussed by .1. S. Fruton and S. Simmonds. I. M. Klotz describes “The Nature of Some Ion-Protein Complexes.― In a very interesting paper en titled “SomeConsiderations of the Interaction of the Metal Peptidases with Their Substrates,― E. Smith and R. Lumry discuss the forces that are involved in enzyme substrate complex formation and the factors affecting peptide hydrolysis. Two papers should be of special in terest to those who are concerned with cancer research. studies on “The Liver Proteins― and the effect of carcinogens on liver components. The last paper by P. C. Zamecnik and I. D. Frantz is concerned with radioactive tracer experi ments on Malignant “Peptide Tissues.― Bond Synthesis in Normal and Many of the papers present information which as yet is not found elsewhere, others give conclusions already published in detail. The discussion that follows each paper and the freedom of expression that the symposium offered give Volume 14 an added value. Metabolism and Function. D. NACHMANSOHN, ED. New York: Elsevier Publishers, 1950. Pp. 848. $7.00. This book is a collection of 88 scientific papers, pub lished originally as Vol. 4, pp. 1—848,of Biochitnwa et Biophysica Ada, in honor of Otto Meyerhof on the oc casion dealing with “Physicaland Chemical Studies of Grami cidin of the same protein from different individuals within limits. Universityof Wisconsin down of Proteins,―K. Linderstrom-Lang discusses the role of denaturation in the enzymatic hydrolysis of pro teins. of similar MARK A. Smins@r sulin molecule is built up of four open polypeptide chains. The quantitative analysis of amino acids in in sulin and lysozyme is discussed by C. Fromageot. In a paper of different preparations Department of Bioc/iemi4ry ture of Insulin,―from which it is concluded that the in stimulating constants the applies.- tion to silk fibroin. F. Sanger summarizes his interesting results on “SomeChemical Investigations mentation proteins and the association and dissociation reaction of protein units. The results suggest that the composition In one of those, J. M. Luck describes The success that has been realized in sepa acids and polypeptides by countercurrent “Chromatographic teins,―K. 0. Pedersen discusses variations in the sedi of his 65th birthday. There are 28 papers in English, 5 in German, and 5 in French. With one or two exceptions, all papers include of Proteins.― A paper on “X-RayAnalysis and Protein Structure―by Dorothy Crowfoot Hodgkin gives a good summary of adequate summaries in all three languages. bibliographies are also given. Six photographs, Adequate including 150 Downloaded from cancerres.aacrjournals.org on June 12, 2017. © 1951 American Association for Cancer Research. Amino Acids and Proteins: Cold Spring Harbor Symposia on Quantitative Biology, Vol. 14. New York: The Biological Laboratory, Cold Spring Harbor, 1950. Pp.217.$7.00 Mark A. Stahmann Cancer Res 1951;11:150. Updated version E-mail alerts Reprints and Subscriptions Permissions Access the most recent version of this article at: http://cancerres.aacrjournals.org/content/11/2/150.1.citation Sign up to receive free email-alerts related to this article or journal. To order reprints of this article or to subscribe to the journal, contact the AACR Publications Department at [email protected]. To request permission to re-use all or part of this article, contact the AACR Publications Department at [email protected]. Downloaded from cancerres.aacrjournals.org on June 12, 2017. © 1951 American Association for Cancer Research.