ANTI-ENZYME IMMUNITY 303 



At 37 °C. the testicular protein appear to exercise a greater affinity 

 for the X-component than the latter exercises for the active lipid-like 

 substance of staphylococcal material. Under these conditions the 

 testicular protein would give the appearance of exercising the role of 

 an activator by combining with the staphylococcal X-component and 

 setting free the lipid-like active substance to convert prothrombin to 

 thrombin. 



Differences in the degree of clotting of various plasmas can likewise 

 be explained by differences in the affinities of species serum proteins for 

 the staphylococcal X-component. This is not an unusual behavior, for 

 it has been shown that cat, horse, human and rabbit etc. sera show 

 different degrees of affinities for a given substance. There is also sharp 

 demarcation among the affinities exercised for a variety of given sub- 

 stances by various components of the serum of a species. Within a 

 given bacterial cell there reside various enzyme proteins with varying 

 or absence of affinities for a chemotherapeutic drug (see further 

 Sevag, 1946). 



In summary it would appear that the above considerations at present 

 do not lend support to the postulated enzyme nature of the staphylococ- 

 cal clotting complex. The data may suggest that it is a lipid-complex. 



6. Antibody Against Rennins 



a. Certain Properties of Rennin. Rennin, found in the gastric juice 

 of the fourth stomach of the calf, catalyzes the clotting of milk. Pepsin, 

 at faint acidities, and chymotrypsin at neutrality also clot milk. Rennin 

 differentiates itself from pepsin by its stability at pH 9.0. At this pH 



termined the degree of dissociation of hemagglutinated systems at 37°C. 25 °C. 

 15°C. and 5°C. They found that the rate of agglutination between the specific serum 

 and red blood cells increases as the temperature at which the reaction takes place 

 is lowered. In going from 37°C to 5°C the equihbrium is displaced and the degree 

 of agglutination at 37°C was found to be about one-third of that at 5°C. 



The results of a study on the energy relationships of the agglutination reaction 

 involving red blood cells by Filitti-Wurmser and Jacquot-Armand C 1947c) show 

 that this is a reversible reaction and obeys laws of mass action. The equilibrium be- 

 tween blood corpuscles and the agglutinins varies with the temperature in the direc- 

 tion corresponding to an exothermic reaction. A calculation by Filitti-Wurmser, 

 Jacquot-Armand and Wurmser (1948) of the ratio of the equilibrium constant 

 K at 25°C. to K at 37°C. K25°/K37°, yielded a value of 3.5 which is said to cor- 

 respond to an enthalpy of — 19000 calories. Assuming that the combination between 

 a molecule of agglutinin and a blood corpuscle is through hydrogen bonds, this 

 energy is said to correspond to three to four of such bondings per molecule of 

 agglutinin. 



