498 Transactions of the Canadian Institute. [Vol. VII. 



fibrin ; he rejected the term zymom given by Taddei, and also that of 

 plant albumin of Berzelius, in the latter case because solubility in water 

 is a characteristic of albumins. The portion soluble in alcohol he called 

 plant gelatin, and considered it to be a casein-like compound of a 

 proteid with an undetermined organic acid. 



Bouchardat^ found in gluten a substance soluble in extremely 

 dilute acid, which he named albumin, since he regarded it as forming 

 the chief constituent of egg albumin, blood fibrin, casein and gluten. 



Dumas and Cahours^^ found four proteids in flour, namely, an 

 albumin which was obtained from the water used in washing out the 

 gluten ; plant fibrin left as a residue on extracting gluten with alcohol ; 

 a proteid from this alcohol which separated on cooling, and finally a 

 second proteid which precipitates from the same alcohol on concentration 

 and cooling. This latter he called glutin. 



Mulder^^ prepared plant gelatin by extracting gluten with alcohol, 

 fihering hot, allowing to cool and redissolving the white precipitate 

 which settled out twice. This he considered to be a compound of 

 sulphur with protein, and he found that it did not contain phosphorus. 



Von Bibra^^ stated that on exhausting gluten with hot alcohol 

 insoluble plant fibrin remained behind, while plant gelatin and plant 

 casein dissolved ; the plant casein separated on cooling. These bodies 

 he thought had the same elementary composition, and were in fact 

 isomers. 



Giinsberg^^ )^q\(^ that gluten was composed of three proteids, gliadin 

 being a mixture of two. These were, (a) gluten fibrin, soluble neither in 

 alcohol nor warm water ; (b) gluten casein, insoluble in hot water but 

 soluble in alcohol ; (c) gluten gelatin, soluble in alcohol and hot water. 



Ritthausen^^ found four proteids in gluten, namely, gluten casein, 

 gluten fibrin, plant gelatin or gliadin, and mucedin, of which the last 

 three are soluble in dilute alcohol. His casein was prepared by ex- 

 tracting gluten with boiling alcohol, cooling, exhausting the casein 

 which settled out with absolute alcohol, then with acetic acid, and finally 

 neutralizing the clear filtrate from this with ammonia. The decanted 

 alcoholic fluid from the casein contained the gelatin, which separated on 

 evaporation. 



Scherer^^ digested gluten with artificial gastric juice and observed 

 that the greater part went into solution in about fourteen hours. 



Martin^^ found that only one proteid was extracted from gluten by 



