92 PHYSIOLOGY [BoT. Absts., Vol. VIII, 



stoff. [The nitrogen changes in germinating lupines with special reference to the relation of 

 formol-titratable and of formalin nitrogen to total nitrogen content.] Biochem. Zeitschr. 93 : 

 253-254. 1919.— A brief note on the S0rensen formol titration method, showing that in the 

 presence of neutral aqueous formaldehyde solution, plant albumins, albuminates, and hemi- 

 albumoses are practically insoluble, while formalin nitrogen, peptone, diastase, etc., remain 

 soluble. Progressive germination gave increased values of formol-titratable nitrogen (sol- 

 uble amino acids), and a corresponding falling off in formalin nitrogen (insoluble protein). 

 The sum of the values obtained approximates the total nitrogen content. — W. W. Bonus. 



METABOLISM (ENZYMES, FERMENTATION) 



641. BoKORNY, T. Bindung des Formal dehyds durch Enzyme. [Formaldehyde fixation 

 by enzymes.] Biochem. Zeitschr. 94: 69-77. 1919.— Reviewing briefly some results of Neu- 

 BERG showing variation in inhibitory effects of different concentrations of formaldehyde on 

 various enzymes, and in the effects of the same concentration on different enzymes, Bokorny 

 accounts for these on the theory of differences in molecular structure of enzymes, with corre- 

 sponding difference in chemical reactions with formaldehyde. Quantitative data are pre- 

 sented showing the effect of formaldehyde on emulsin, based upon the formation of hexa- 

 methylenetetramine when formaldehyde reacts with ammonia, 6 HCOH + 4 NH3 = 6 H2O + 

 C6H12N4. Any excess ammonia is titrated against sulphuric acid. Treating 1 g. emulsin 

 with 50 cc. 0.925 per cent formaldehyde for 3 days showed a formaldehyde combination of 

 11-38 per cent of the dry weight of the enzyme. The results cited are followed by the author's 

 views on the protein nature of the enzyme, as indicated by its amphoteric properties, com- 

 bination with acids, bases, etc. — W. W. Bonus. 



642. BoTJRQTJELOT, Em., M. Bridel, et a. Aubry. Synthase biochimique du cellobiose 

 a I'aide de I'emulsine. [Biochemical synthesis of cellobiose by means of emulsin.] Jour. 

 Pharm. et Chimie 21: 129-132. 1920.— Cellobiose or cellose is a glucobiose and is isomeric 

 with gentiobiose and maltose. The authors succeeded in synthesizing this sugar by allowing 

 emulsin to act on a 50 per cent aqueous solution of glucose. The formation is probably due 

 to the fact that emulsin does not appear to be a uniform ferment but to be composed of gentio- 

 biase, cellobiase, and beta-glucosidase. — H. Engelhardt. \ 



643. Bridel, M. Sur la resistance des ferments de I'emulsine a Paction prolongee de 

 I'alcool methylique k 70 p. 100. [The resistance of emulsin toward the prolonged action of 70 

 per cent methyl alcohol.] Jour. Pharm. et Chimie 22 : 323-327. 1920.— Seventy per cent 

 methyl alcohol did not destroy the fermentative power of emulsin on beta-glucosides, lactose, 

 and beta-ethyl-galactoside within 5 years. The strength, however, had been considerably 

 reduced. The ferments acting on lactose and beta-ethyl-galactoside appear to be more resis- 

 tant than beta-glucosidase. — H. Engelhardt. 



644. Falk, K. G. The chemistry of enzyme actions. Amer. Chem. Soc. Monogr. Ser. 

 136 p. Chemical Catalog Co. : New York, 1921. — This constitutes the first of a series of mono- 

 graphs proposed by the American Chemical Society. These monographs are designed to 

 serve two purposes, (1) to present in readable form for those who may not be specialists in 

 the particular field the knowledge available on the selected topic, and (2) through a well 

 digested survey of the present status of the problem to promote and facilitate research. 

 The author is convinced that enzyme studies make contributions not merely to the chemical 

 phenomena underlying living matter" but also to "a better understanding of the fundamental 

 chemical relations underlying an exact knowledge of chemical reactions." — He recognizes 

 2 methods of attack, briefly, (1) enzymes as catalysts, modifying reaction velocities (the 

 kinetics of enzyme action), and (2) the chemical nature of enzymes and their reactions. He 

 purposes to indicate the progress attained by these 2 methods, and proceeds to develop the 

 subject under the following captions: Velocities of chemical reactions; general theory of chem- 

 ical reactions, catalysis; chemical reactions catalyzed by enzymes; physical properties com- 

 mon to enzyme preparations; chemical properties common to enzyme preparations; chemical 



