THE CHEMICAL CONSTITUTION OF ITS UNITS 33 



Leucine. 



A substance, corresponding to our leucine, was described by Proust 

 in 1818 under the name of oxide-caseux. Two years later, in 1820, 

 Braconnot isolated from the products resulting by boiling meat with 

 dilute sulphuric acid a substance which he named leucine on account 

 of its glistening white (Xev^o?) appearance. Mulder, in 1839, obtained 

 it by boiling meat with alkali and by the putrefaction of casein. Its 

 occurrence and oxidation products were investigated by Liebig, who 

 regarded it as one of the constituents of the protein molecule, as was 

 proved in 1849 by Bopp, who prepared it from caseinogen, fibrin and 

 albumin by fusion with potash, by hydrolysis with acids and by putre- 

 faction. Hinterberger showed that it was present in horn, and Zolli- 

 kofer in elastin. 



Leucine also occurs in the free state in the various organs of the 

 animal body as pointed out by Frerichs and Stadeler and many other 

 observers. 



Not only is it present in the animal proteins, but also in the vegetable 

 ones, from which it passes by the action of enzymes into the extracts of 

 germinating seedlings, as shown by Schulze and his co-workers. Leu- 

 cine is, with the exception of arginine, the most widespread of all the 

 amino acids which go to make up the protein molecule. 



Its correct empirical formula C 6 H 13 NO 2 was first given to it by 

 Laurent and Gerhardt. These observers and also Cahours showed that 

 it belonged to the glycine series of compounds ; Liebig and others 

 showed that on oxidation it gave ammonia and valerianic acid, and 

 also valeronitrile, and Strecker obtained leucic acid by treating it with 

 nitrous acid. But only in 1868, when Hiifner obtained caproic acid 

 and ammonia by reducing it with hydriodic acid, was it shown to be 

 an a-aminocaproic acid. Hufner tried to prove this by comparing the 

 natural leucine with two synthetical leucines, (i) that prepared by the 

 action of ammonia on bromocaproic acid obtained from the fermentation 

 caproic acid, and (2) that prepared from isovaleraldehyde, hydrogen 

 cyanide and ammonia which had been first synthesised by Limpricht in 

 1855. Neither of these two synthetical leucines corresponded exactly 

 with natural leucine, and Hufner, rather than regard them as isomers, 

 regarded them as identical compounds. 



The question of the constitution of leucine was again taken up in 

 1891 by Schulze and Likiernik. The natural product is optically 

 active, but by heating with baryta at 1 60 C. it is racemised ; this 



inactive leucine, on being compared with the leucine prepared from 

 PT. i. 3 



