CHEMICAL BASIS OF THE ANIMAL BODY. 39 



into leucin, ty rosin, &c., each peptone being preceded by a correspond- 

 ing anti- or hemi-albumose. Antipeptone remains as antipeptone even 

 when placed under the action of the most powerful trypsin, provided 

 putrefactive changes do not intervene. Kiihne's views may be conve- 

 niently exhibited in the accompanying tabular forms. 



DECOMPOSITION OF PROTEIDS BY ACIDS. 



1. 

 By -25 p. c. HC1 at 40 C. 



Albumin. 



Antialbumate. Hemialbumose. 



:ialbumid. 



Antialbumid. Hemipeptone. Hemipeptone. 



2. 



By 35 p. c. H 2 SO 4 at 100 C. 

 Albumin. 



Antialbumid. Hemialbumose. 



l 



Hemipeptone. Hemipeptone. 

 Leucin. Tyrosin. etc. Leucin. Tyrosin. etc. 



DECOMPOSITION OF PROTEIDS BY DIGESTIVE FERMENTS (ENZYMES). 



Albumin. .8 



Antialbumose. Hemialbumose. 



I I 



Antipeptone. Antipeptone. Hemipeptone. Hemipeptone. 



Leucin. Tyrosin. Leucin. Tyrosin. 

 etc. etc. 



v. 



The several products (antipeptone, &c.) are given in duplicate, on 

 the hypothesis (of which there is now but little doubt) that the changes 

 of digestion are essentially hydrolytic changes, accompanied by a 

 deduplication ; that just as a molecule of starch splits up into at least 

 two molecules of dextrose, or as a molecule of cane-sugar splits up into 

 a molecule of dextrose and a molecule of levulose, so a molecule of 

 antialbumose, for instance, splits up into at least two molecules of 

 antipeptone, and so on. 



