420 CHEMICAL DYNAMICS 



the value of p for hydrolysis by a given enzyme varies with the 

 nature of the substrate. (Cf. table in Arrhenius' work, loc. cit., 

 pp. 99-98.) 



The influence of temperature upon the coagulative power of 

 rennet has been studied by Fuld (32) ; here also the van't Hoff- 

 Arrhenius' rule holds good; /* is 20,650. 



The interesting observation has been made by Cesana (17) in 

 studying the influence of temperature upon the ultramicroscopic 

 appearance of trypsin solutions, that the optimum temperature 

 for its proteolytic activity corresponds with that at which there 

 is a minimum of visible granules in the ultramicroscopic field 

 and a maximum dispersion of the trypsin leading to a maximum 

 frequency of collisions between trypsin particles or molecules 

 and the molecules of the substrate. 



LITERATURE CITED 



(1) Acree, S. F., Amer. Chem. Journ., 39 (1908), p. 513. 



(2) Anders6n, H. C., Biochem. Zeit., 70 (1915), p. 344. 



(3) Arrhenius, S., "Immunochemistry," New York (1907). 



(4) Bang, I., Zeit. f. physiol. Chem., 43 (1904), p. 358. 



(5) Bayliss, W. M., Arch, des Sc. Biol. Petrograd, 2 Suppl. (1904), p. 261. 



(6) Berg, W. N., and Gies, W. J., Journ. Biol. Chem., 2 (1907), p. 489. 



(7) Berninzone, Atti. del soc. ligi. di Scien. nat. e geograph. Genoa, 11 



(1900), p. 327.. 



(8) Berzelius, J., Jahresber. ueber die Fortschr. der physischem Wiss., 



13 (1836), p. 237; 20 (1841), p. 452. 



(9) Bodenstein, M., and Dietz, W., Zeit. f. Elektrochem., 12 (1906), 



p. 605. 



(10) Bogdandy, S. von, Zeit. f. physiol. Chem., 84 (1913), p. 18. 



(11) Borissov, P., Arch, des Sc. Biol. Petrograd, 2 (1893), p. 699. 



(12) Bosworth, A. W., Journ. Biol. Chem., 15 (1913), p. 231. 



(13) Bosworth, A. W., Journ. Biol. Chem., 19 (1914), p. 397. 



(14) Bradley, H. C., Journ. Biol. Chem., 8 (1910), p. 251. 



(15) Brseunning, H., Zeit. f. physiol. Chem., 42 (1905), p. 70. 



(16) Bubnow, N. A., Zeit. f. physiol. Chem., 7 (1883), p. 315. 



(17) Cesana, G., Archivio di Fisiologia, 11 (1913), p. 130. 



(18) Chittenden, R. H., and Cummins, A. W., Trans. Connecticut Acad. 



of Sci., 7 (1885), p. 108. 



(19) Clement, M., and D<sormes, M., Ann. de Chim., 59 (1806), p. 329. 



(20) Conroy, J. T., Journ. Soc. Chem. Ind., 21 (1902), p. 302. 



(21) Coppadore, A., Gaz. Chim. Ital., 31 i (1901), p. 425. 



(22) Cramer, M., Ber. d. d. chem. Ges., 32 (1899), p. 2062. 



(23) Dauwe, F., Beitr. z. chem. Physiol. und. Path., 6 (1905), p. 426; 7 



(1905), p. 151. 



