LECTURES ON IMMUNITY 



Trypsin behaves in a manner very similar to that of 

 rennet and pepsin. The reaction of the spontaneous 

 attenuation is monomolecular and the velocity constant 

 of reaction increases very rapidly with temperature 

 (//. = 62,000). The values are given below: 



K = 0.0031 7. (j. = 62,034. 



The concentration of the trypsin solution exerts no 

 sensible influence on the rate of destruction in this case. 

 Solutions containing 2, 4, 6, 8, or 10 per cent of trypsin 

 all gave satisfying results when calculated with the 

 value K= 0.0073 (at 67.15 C). The strength of the 

 trypsin was measured by means of its property of liquefy- 

 ing thymolgelatin. 



Trypsin exerts, as we saw, a destructive influence on 

 coli-agglutinin, and this destruction proceeds faster at 

 higher temperature than at lower, as is seen from the 

 following measurements of Madsen and Walbum. At 

 44.2 C. the calculated values differ for some time rather 



