370 EXPERIMENT STATION RECORD. 



coutaining from 90 to 50 per cent of it, together witli from 10 to 50 per cent of 

 leiicosin, are not distinguishable by analysis. 



"(4) A piotoproteose less readily precipitated by alcohol than the preceding, and 

 of a different comj»ositiou , as shown by the following figures: 



Malt protoproteoiic . 



Per cent. 



Carbon 50. 63 



Hydrogen 6. 67 



Nitrogen - 16. 69 



S"lP^"^ !■ 26.01 



Oxygen . I 



100. 00 



"That this is not an imjinre preparation of the preceding, is indicated by the fact 

 that the aniouut of nitrogen is alil<o, in both, while the carbon differs l>y 2 per cent. 

 This difference would probably not be caused by nou-proteid impurities. It is pos- 

 sible that the dcnteroproteose, next to be described, may not have lieen completely 

 separated by the process employed. 



"(5) A deuteroproteose which could not be separated froui non-proteid impu- 

 rities. 



"(6) A heteroproteose in extremely small amount. 



"(7) Byniii, aproteid insolul)leiu water and saline solutions, but readily soluble in 

 dilute alcohol. About 1.25 per cent of this proteid was obtained from the malt, 

 having tin; following composition : 



Jiynin. 



Per cent. 



Carbon 55. 03 



Hydrogen 6. 67 



Nitrogen 16. 26 



Sulphur 0. 84 



Oxygen 21 . 20 



100. 00 

 "(8) A proteid insoluble iu water, in salt solution, and in alcohol, amounting to 

 3.80 per cent. The couipositiou and properties of this proteid we have been unable 

 to determine. 



"Assuming 21 per cent of the total niti'ogen of the malt to exist in non-proteid 

 bodies, and admitting the malt proteids to contain on the average 16.3 per cent of 

 nitrogen, we have, in the malt investigated, a total of 7.84 per cent of proteids. 



Per cent. 



Proteid, insoluble in salt solution and in alcohol 3. 80 



liynin, soluble iu dilute aliohol 1. 25 



Bynedestin, leucosin, and i)roteose8 soluble in water .and salt solu- 

 tion: 



Coagulable 1. 50 



Uncoagulal)le 1. 29 



Total proteids 7. 84 



"The results of this study show: That, in germination, the proteids of barley 

 undergo extensive changes without acquiring, or before acquiring, the properties of 

 proteoses; that hordein disappears and an alcohol-soluble proteid of entirely differ- 

 ent composition takes its place; that edestin also disappears and a new globulin is 

 formed, very different both in composition and properties. The albumin, on the 

 other hand, appears to be unchanged in its characters, but its quantity is increased. 

 It is to be noted also that hordein and edestin are both rejilaced by proteids much 

 richer in carbon and poorer in nitrogen." 



