80 LECTURES ON IMMUNITY 



agree very closely with the observed ones. The same is 

 the case for the digestion of the solution of egg-white, 

 which had been previously heated to 100 C. in order to 

 destroy its content of antitrypsin. The solution contained 

 10 c.c. of a mixture of 10 per cent of egg-white and 90 per 

 cent of distilled water, and further i c.c. of a i per cent 

 solution of trypsin. Here KP = 30. The reaction with 

 casein increases (the determination is not very reliable) 

 in the proportion i : 5.3 between 20.7 and 30.7 C. 

 = 29,500) and 1:2.6 between 30.7 and 38.7 and has 

 probably an optimum, due to the instability of trypsin at 

 higher temperature. 



In this case the increase of conductivity depends prob- 

 ably on the formation of ammonium salts of the reaction- 

 products. These also react with the trypsin, so that the 

 quantity of free trypsin is nearly inversely proportional to 

 the quantity of reaction-products, whereby the reaction 

 progresses proportionally to the square root of the time 

 in its first period. Bayliss showed that the addition of 

 digestion-products, as well as asparagin, glycin (Merck), 

 leucin, and amphopepton (Griibler), retards the action of 

 trypsin to a high degree. 



Henri and Larguier de Bancels l have used the method 

 of Sjoqvist for the study of digestion by pancreatic juice. 

 They found that this process of tryptic digestion follows 

 the laws for monomolecular reactions and give as an illus- 

 tration the following figures for the changes in the 

 conductivity with time (at 44, 4 per cent solution of 

 gelatine). 



1 Victor Henri and Larguier de Bancels : C. JR. de ta Soc. de Biol. 55. 

 787, 789, and 866 (1903). 



