MECHANISM OF PROTEIN HYDROLYSIS AND IMMUNIZATION 43 



effects the hydrolysis or oxidation of each molecule of allantoin 

 (by removal of two molecules of CO 2 and substitution of a 

 molecule of H 2 O) into two molecules of urea, CH 4 N 2 O, the 

 ultimate waste product of purin-bearing proteins. 



If this assumption is valid, a still clearer view is gained of the 

 modus operandi of non-specific proteins as therapeutic agents in 

 dealing with rheumatoid conditions (commonly believed to be 

 associated with the inadequate catabolism of purin bodies and 

 their oxidation product, uric acid), and with malignant neoplasms, 

 the structure of which is largely made up of purin-bearing pro- 

 teins. An agent which stimulates production of red corpuscles 

 and enhances their enzymic activities, as the non-specific pro- 

 teins have been amply demonstrated to do in my hands and 

 those of my associates, should theoretically be effective in pre- 

 cisely those conditions in which the proteals have been observed 

 to have clinical value. 



Further consideration of this aspect of the subject must be 

 deferred, however, until we have dealt with the more general 

 fundamental properties concerned. Taking up the sequence of 

 the original presentation of the Proteomorphic theory, we may 

 advantageously make inquiry as to the extent to which foreign 

 proteins are present in the parenteral system under usual 

 conditions. 



PROTEOLYTIC ACTIVITIES OF THE LEUCOCYTE 



It has been shown by various experimenters (Voit and Bauer, 

 Haidenhain, Friedlander, Waymouth Reid, Ascoli and Vigano) 

 that, under certain conditions, unmodified food proteins may find 

 their way through the intestinal walls and enter the general cir- 

 culation. It is against these, according to the present view, that 

 the digestive functions of the various types of leucocyte are exer- 

 cised; the work of the leucocyte with these, as with the bacterial 

 proteins, being a work of proteolysis strictly comparable to that 

 performed by the digestive ferments in case of proteids in the 

 digestive tract with certain variations to be noted. 



This view finds strong support in the fact that one at least 

 of the enzymes found in the body of the leucocyte is closely com- 

 parable to, if not identical with, the trypsin of the digestive 

 canal. It is possible, according to some experimenters, that syn- 

 thetic activities also lie within the capacities of these enzymes 

 (all catalytic phenomena are conceivably reversible). But, as- 

 suredly, their habitual province is to break down or cleave this 

 protein molecule, not to synthesize it. 



It is known that the unbroken food protein, and even so small 

 a cleavage product as peptone, do not exist normally in the 



