ARTICLES 431 



physically or chemically, so also a physico-chemical explanation 

 may be looked for in regard to anti-enzymes. 



There has been much controversy on the subject of anti- 

 enzymes, and the elucidation of their nature has not been made 

 any easier by authors ignoring published work of other observers 

 holding a different view, or referring compromisingly to " so- 

 called anti-enzymes." 



The greatest advocate of the non-existence of anti-enzymes 

 as definite entities is Bayliss (19 19), who bases his argument 

 on his experience when attempting to verify the early work 

 of Hildebrandt, who had claimed to have found an anti- 

 emulsin. 



Bayliss (191 3) showed that the anti-emulsin effect was 

 really due to change in the concentration of the H' ion of the 

 system. He points out also that in the experiments of Ohta 

 (191 3) — ^who likewise claimed to have discovered an anti- 

 emulsin — the latter had not taken into consideration possible 

 changes in the H* ion concentration. 



Taking as an analogy the inactivation of rennet by shaking 

 — a phenomenon probably due to surface coagulation — Bayliss 

 notes too that substances capable of adsorbing enzymes may 

 reduce their action by causing a reduction in their concentra- 

 tion. In this he is supported by the fact that anti-enzymes 

 are related to the albumin factor of proteins and not to the 

 globulin factor, as is the case with antibodies formed as a result 

 of the injection of bacteria or other toxins. 



The work of Jahnson-Blohm (1912) gives support to the 

 above suggestion. This investigator showed that anti-enzyme 

 action could be prevented by a more strongly adsorbed sub- 

 stance. Such a substance, e.g. saponin, unites with that 

 body which otherwise would adsorb the enzyme. 



Several observers other than Bayliss have failed to obtain 

 increased anti-ferment action in serum on the injection of 

 foreign protein, while some, e.g. Visco (191 5), have been unable 

 to demonstrate anti-enzyme (anti-trypsin) action in normal 

 blood, if other factors were excluded. 



Dezani (191 6) was unable to find antipepsin in the blood, and 

 he points out that inactivation of pepsin (in vitro) is due to the 

 alkalinity of the serum, and that if hydrochloric acid be added 

 retardation of action may still be caused by a deficiency of free 

 acid. 



Young (191 8) could not find increased anti-tryptic action 

 in the blood serum after the injection of trypsin, although for- 

 mation of the usual precipitins for the proteins injected was 

 noted. Linossier (191 6) observed that the already great anti- 

 peptic properties of horse serum are increased by heating ; 

 further he found that egg-white and gelatine are antipeptic, 



