BY MEANS OF CATALYSTS. CREIGHTON. 33 



glucoside into their antipodes by means of emulsin. Of these 

 two isomers only the /3- form is attacked by emulsin, which 

 conversely this form is not changed by yeast and the a- anti- 

 pode is split up into grape sugar and methyl alcohol. This 

 "lock and key" relationship between enzyme and substrate has 

 been confirmed by Pottevin 1 and others 2 . 



This stereochemical specificity of enzymes has been held to 

 be a fundamental difference between the ordinary catalysts and 

 the enzymes, and an important reason why the latter should 

 not be looked on as catalysts. Very recently, however, this 

 argument has been broken down by the investigations of Bredig 

 and Fajans-' 5 whose results show that ordinary catalysts of 

 asymmetric structure may, like enzymes, also possess a stereo- 

 chemical specificity. The results, which I have obtained in 

 the present investigation, confirm and strengthen this new and 

 important relationship between enzymes and ordinary satalysts. 



SUMMARY. 



1. The decomposition of bromcamphor-carboxylic acid in 

 acetophenone solution has been investigated kinetically, and it 

 has been found that the presence of small quantities of alkaloids 

 accelerate this decomposition enormously. 



2. Optically active bases catalyse the decomposition of the 

 antipodes of the acid in different degrees. The difference 

 between the velocities of decomposition of the two optical- 

 isomeric acids is as much as 30^ in some cases (Tables V and 

 VI). 



3. This catalytic behaviour of optical active bases suggests 

 an analogy to the st&reo chemical specificity of the enzymes. 



1. Pottevin, H.: Compt. rend., 136, 169, (1903). 



2. For an account of the numerous investigations in this field, 

 Fajans, K., loc. cit. 



3. Fajans, K. : loc. cit. 



I 'HOC. & TKANS. X. S. I. VST. Sri.; Vol.. XIII. TKANS. 3. 



