574 Drs. T. A. Henry and 8. J. M. Auld. [July 22, 
and to measured portions of the mixture a weighed quantity of commercial 
preparations of pepsin, trypsin, and papain were added. After a certain 
period had elapsed, portions of these mixtures were allowed to act on 
solutions of amygdalin, and the amounts of hydrocyanic acid formed after 
definite periods were determined. 
As a control experiment, 20 c.c. of the emulsin mixture were allowed to 
stand, and at intervals 2 c.c. were added to 1 gramme of amygdalin dissolved 
in 20 cc. of water, and the amount of the glucoside decomposed estimated 
after a certain lapse of time. 
Control Experiments with Emulsin. 
Time allowed | Time of action on Amygdalin decomposed. 

to stand. amygdalin. 
hours. | hours. Per cent. 
— 18 65 °7 
25 18 63 °*2 
50 18 56 °8 

Experiments with Emulsin and Proteolytic Enzymes. 
| 

yy PAN Weight = Volume Time Time of action Asavodaln 
y of proteolytic | of emulsin of proteolytic of emulsin d ys d 
Fe aa | luti tion on amygdalin mie 
enzyme. | solution. action. yg 
gramme. C.C. hours. hours. Per cent. 
OPsiNy cece: 0:2 3 26 24: None 
3 50 [2—3 days] 3 
0:2 5 25 24, 2°0 
5 50 48 None 
0°2 20 24 18 32 °0 
20 50 24 Savi 
20 106 24, None 
Trypsin ...... 0:2 3 26 24 47 °3 
3 50 24: 33 0 
0°2 5 25 24 51°3 
5 50 24 38 °O 
Papain ...... 0:2 5 24, 18 60 °7 
5 50 24, 58 °3 



These results show that, of the three proteolytic ferments used, pepsin 
exerts a powerful destructive action on the activity of the emulsin of almonds, 
trypsin a well-marked action, whilst papain affects it slightly. It will be 
observed that the slight action exerted by trypsin on emulsin is similar to 
that of the proteolytic enzyme of yeast on the glucosidolytic constituent of 
yeast, and this is in conformity with Kutscher’s observation* that the proteo- 
* © Zeit. Physiol. Chem.,’ 1901, vol. 32, p. 59. 
