464 



SCIENCE. 



[N. S. Vol. XX. No. 510. 



dicates a beginning, as there is an almost 

 ^unexplored gap between northern California 

 and Prince William Sound, while among the 

 Aleutian Islands pycnogonids are rather abun- 

 dant, and would probably, on thorough ex- 

 ploration, add considerably to the number of 

 four species now known from that region. 



The book concludes with an excellent index 

 and well sustains the high reputation which 

 the earlier volumes of this important series 

 liave maintained. 



W. H. Dall. 



Smithsokian Institution. 



Chemie der Eiweisskorper. Von Dr. Otto 

 COHNHEIM, A. o. Professor an der Univer- 

 sitat Heidelberg. Zweite vollstandig neu 

 bearbeitete Auflage. Braunschweig, F. 

 Vieweg und Sohn. 1904. 

 The first edition of Cohnheim's ' Chemie der 

 Eiweisskorper,' published in 1900, speedily 

 gained a wide circulation among physiological 

 chemists and won for itself a place as a most 

 useful book of reference. No other compre- 

 hensive and satisfactory compilation of the 

 literature on proteids had been attempted since 

 Drechsel's article in Ladenburg's ' Handwor- 

 terbuch,' published in 1885. The appearance 

 of a new edition by Cohnheim, so completely 

 revised in some parts that it almost deserves to 

 be called a new book, testifies the popularity 

 which the work has enjoyed and above all the 

 rapid progress which the study of proteid 

 chemistry has made in this brief period of 

 four years. An era of classification in which 

 new proteids were isolated and their physical 

 and chemical properties investigated, has been 

 followed by renewed interest in the chemical 

 structure of the albuminous substances. The 

 recent fruitful researches of Emil Fischer, 

 Kossel and others bear witness to the advances 

 which improved methods of study can inaugu- 

 rate. Accordingly, we find in the new volume 

 an entire chapter devoted to the chemical con- 

 stitution of the proteids. This, as well as 

 other parts of the book, is characterized not 

 only by the completeness and accuracy of the 

 list of references to the literature, including 

 the earlier pioneer work, but also by the exer- 

 cise of critique in the presentation of such 

 detailed data. It is this selective and un- 



biased treatment which makes a compilation 

 readable. 



Without attempting any detailed review, it 

 may be of interest to refer to some of the more 

 noteworthy changes or innovations in the 

 present edition. The molecular structure 

 characteristic of the proteids and serving to 

 define thenr is summarized in the following 

 words : 



Die wichtigste Gruppierung ist nun sielier die 

 obeii besproehene Siiureamidbindung der a-Amido- 

 siiuren, und man kann daraufhin KOrper wie das 

 Glycylglycin iind seine Homologen als die ein- 

 fachste EiweisskSrper bezeiehnen. Richtiger ist 

 es aber wohl, Kossel zu folgen, und auch die zweite 

 Verbindungsform, wie sie Im Arginin vorliegt, als 

 notwendig fur den Eiweissbegriff anzusehen. 

 Danaeh hat man als Eiweisskorper Saureamide 

 aus a-Amidosiluren zu bezeiehnen, von denen eine 

 das Arginin ist. 



Unter diese Definition fallen zweifellos alle Pep- 

 tone und auch die komplizierteren Peptide, ebenso 

 die Protamine, deren Abtrennung von den Eiweiss- 

 korpern bei den breiten chemischen und genet- 

 ischen Ubergangen zwischen ihnen und den an- 

 deren Eiweisskiirpem durehaus willkurlich 

 erseheint. Die von Low und Hofmeister versuchte 

 Heranziehung des physiologisehen Elementes hat 

 bei einer chemischen Definition Bedenken und ist 

 unzulassig, seit es wahrscheinlich geworden ist, 

 dass der Tierkorper sein Eiweiss aus alien stick- 

 stoffhaltigen Verbindungen aufbauen kann, die 

 fiir seine Fermente zuganglieh sind (p. 71). 



The discussion of the physical and physico- 

 chemical properties of proteids has been modi- 

 fied to conform with changing ideas. This is 

 especially evident in Chapter V. in the treat- 

 ment of the salt-like compounds of the pro- 

 teids. The twofold behavior of the latter 

 towards acids and bases, assigned in the earlier 

 edition to their character as pseudo-acid and 

 pseudo-base (Hantzsch), has given way to a 

 somewhat different interpretation. The 

 unique combining properties of the proteids 

 are now attributed by the author to the amido- 

 acid complexes which form the molecule, since 

 simple amido-acids are known to show pre- 

 cisely similar reactions. In the classification 

 of the proteids no notable change is intro- 

 duced. Casein is still referred to under the 

 most unsuitable designation of nucleo albumin, 

 not, however, without at length indicating its 

 specific character as a phosphorus-containing 



