224 BIO-CHEMICAL JOURNAL 



enzyme falls ; in other words the more dilute the solution the more 

 adsorption takes place. This is particularly well shown by the last 

 experiment on the table. The mathematical expression given is also 

 in accordance with this interpretation. 



If the union of enzyme and substrate follows the law of adsorption 

 it would be expected that there would be found some effect of this 

 law on the relation of activity of enzyme to its concentration. In my 

 paper on The Kinetics of Tryptic Action, 1 I showed that the form of the 

 function in question varied according to the stage of the reaction, but 

 if we take the early stages in which the action is most rapid there 

 seems to be some effect suggestive of an adsorption process. The 

 initial linear stage is very short, so that we may omit it, and, if we 

 compare the relative times taken by concentrations of trypsin varying 

 as 8, 4, 2, and I to produce an increase of conductivity of 1800 

 gemmhos in caseinogen solution, we find the values are : 



so that the lower concentrations of trypsin are relatively more active. 

 It is somewhat remarkable that the value of the exponent found in 

 another experiment was 1-42 to 1-67* and this is the same as that 

 given by Reichel and Spiro in their paper for the ' Teilungstactor ' of 

 rennet, viz., 1-5 to 1-67. Whether this is merely an accidental 

 coincidence I am not prepared as yet to state, the subject being still 

 under investigation. 



I have myself made one or two experiments similar to those or 

 Dauwe, which are perhaps of sufficient interest to give here. It was 

 shown by W. A. Osborne that calcium caseinogenate does not pass 

 through a porous clay filter, trypsin, on the contrary, does do so. If 

 then, we mix solutions of trypsin and calcium caseinogenate, the 



i.. Archives des. Sciences Biologitjues. Tome XI, Supplt. p. 261. St. Petersburg, 1904.. 

 2. Page 26 of the reprint. 



