ANTIBODIES AGAINST RESPIRATORY ENZYMES 395 



hibitory effect of the immune sera, they also experimented with dia- 

 lyzed sera. 



Table XXI 



In confirmation of Gessard's observation, they found that this anti- 

 body is not destroyed by heating to 60°C. Heating at 80°C. destroyed 

 it completely. They also observed that while the anti-laccase serum 

 inhibited laccase strongly, normal serum accelerated its activity. In 

 conclusion, they stated that the inhibition of laccase by homologous 

 immune sera does not depend on the presence of any of the known 

 laccase inhibiting factors. 



Adams (1942) experimented with a preparation of tyrosinase from 

 the domestic mushroom, Psalliota campestris. Its activity was 500 

 catechol-hydroquinone units per mg. dry weight. The copper content 

 was 0.13 per cent of the dry weight of the enzyme. The immune rabbit 

 serum prepared against the enzyme reacted with the antigen in 

 1 : 500,000 dilution. Normal sera were inactive. The tyrosinase from 

 the mushroom Lactarius fiferatus failed to show any cross precipitin 

 reaction with the antiserum to the Psalliota caiwpestris tyrosinase. 

 Adams stated that in no case did the antibody have any effect on the 

 catalytic activity of the enzyme in the mixture. 



Duliere and Adant (1934) reported that the injection of an active 

 tyrosinase (from mealworm) preparation into rabbits modifies the 

 properties of the animal's serum. This serum has an inhibitory effect 

 on a tyrosinase preparation if this is strongly active. The prepared 

 serum, when the injected tyrosinase is very feeble or practically in- 

 active, has no effect on an active tyrosinase. 



