Methods of Enzymology.
Methods of Enzymology.
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DOI：
10.1021/ja01594a086
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发表时间：
1956-07
影响因子：
15
通讯作者：
H. Tauber
中科院分区：
文献类型：
--
作者：
H. Tauber
Methods of Enzymology. Volume II. Editedby Sidney P. Colowick and Nathan O. Kaplan, McCollum-Pratt Institute, The Johns HopkinsUniversity, Baltimore, Maryland. Academic Press, Inc., Publishers, 125 East 23rd Street, New York 10, N. Y. 1955. xx+ 987 pp. 16.5 X 23.5 cm. Price $23.80. This volume is dedicated to the memory of James B. Sumner (1887-1955). There are 5 sections dealingwith enzymes in protein metabolism, nucleic acid metabolism, phosphate metabolism, coenzyme and vitamin metabolism and respiratory enzymes. The 5 sections are further sub-divided into 152 contributions by as many authors, dealing with preparative procedures andassay methods. On p. 48 inthe discussion of trypsin inhibitors the findings of Tauber, Kershaw and Wright [/. Biol. Chem., 179, 1155 (1949)] have been misrepresented. The fact is, Tauber, Kershaw and Wright found (as shown in Table III) the crude Lima bean inhibitor to be4. 5 times more active than the crystalline fraction. It is obvious that the author of this review did not check the original paper but used another source material. On p. 475 thepreparation of non-specific adenosine deaminase from Takadiastase is described. Com-mercial Takadiastase which contains a large quantity of inert material is not good starting material for the preparation of highly active mold enzymes. Natural mixtures of concen-trated enzyme products producedfrom Aspergillus oryzae type mold cultures are now commercially available. Meth-ods have been described for the preparation of soluble enzymes from mold bran cultures. These too are mixtures of a large number of enzymes and are suitable for the prepa-ration of non-specificadenosine deaminase. On pp. 776 and 777 twomethods for the preparation of crystalline beef liver catalase are described in detail. These procedures, however, are not the easiest for the crystallization and re-crystallization of catalase. The more recent methods of Tauber and Petit are now in general use[/. Biol. Chem. 195, 703 (1952); 205, 395 (1953)]. On p. 791 under the heading “Peroxidase (liver),” the preparation of a fraction containing liver proteins is described. This fraction having both catalase and peroxidase activity is said to contain a specific peroxidase because it oxidizes guaiacol. This con-clusion, based on optical measurements, may be correct. It has been shown, however, that crystalline catalase can also oxidize large molecules and this fact should havebeen mentioned by the author. In this volume peptide bond synthesis and transpeptidation by proteolytic enzymes are presented. In this connection the reviewer wishes to call atten-tion to the recent test of Haurowitz and Horowitz [This Journal 77, 3138 (1955)] which employs isotopically labeled substrates to determine enzymatic transpeptidation.Enzymology has grown to enormous proportions in the past 30 years. A large number of important discoveries have been made. The reviewer’s few critical remarks intend to show that even an expertly prepared work such as this does not include all the facts and all of the literature. It requires careful supplementing with past and current source materials. It is the reviewer's opinion that this volume, similar to Volume I, will be gratefully received by enzyme investigators everywhere. Venereal Disease Experimental Laboratory U. S. Public Health Service School of Public Health Henry Tauber University of North Carolina Chapel Hill, North Carolina
