Og2 EXPEEIMENT STATION RECORD, IVol. 3r. 



antigen a greater toxicity is bestowed on the antigen, and that an increase of 

 the antiferment titer in sensitized animals is associated with an increased re- 

 sistance against anaphylactic shock. 



Bacterial antiferments are thought to consist of unsaturated lipoids of the 

 organisms, and the absolute resistance of intact organisms probably depends 

 on a potential lipoid envelopment. Microchemical analysis revealed no increase 

 of nonprecipitatable substances during bacteriolysis. 



Complement and serum protease are not deemed identical. 

 The presence of protease was established in the serum of the guinea pig 

 and rabbit. It was active in weakly acid and in alkaline solutions. Its action 

 was markedly retarded at 56° C. and completely inhibited at 70°, was retarded 

 by unsaturated soaps, and was nonspecific. 



It is indicated that the Abderhalden reaction is accompanied by an adsorption 

 of serum and a ferment. Specific tissue is not cleaved in the reaction, but the 

 cleavage products originate from the serum proteins. 



In the treatment of pathological cases with potassium iodid there is a 

 constant lowering of the antitryptic titer by which the proteolytic ferments of 

 the organism become more active. It is deemed possible that the therapeutic 

 action of potassium iodid depends on this lowering of antiferment content. 



On the serological action of boiled and unboiled milk and milk proteins, 

 A. Versell (Ztschr. Immunitdtsf. u. Expt. Ther., I, Orig., 24 {1915), No. S, 

 pp. 261-291). — Complement-fixation tests with human, cow's, and goat's milk 

 have shown that human milk antisera react with cow's milk and, to a slight 

 extent, with goat's milk. Cow's milk antisera also react with human milk. 

 In a similar manner cow's milk casein antisera and heated cows' milk antisera 

 react with human milk casein and boiled human milk. Contrary to this, there 

 is no reaction between human serum antisera and cow or goat serum, or 

 between cow serum antisera and human serum. The antisera obtained by the 

 injection of milk serum and the casein react much stronger with the whole 

 milk than with the respective constituents used for immunization. Whole milk 

 and milk serum antisera, even in very small quantities, cause complement devia- 

 tion with the blood serum of homologous animals. The casein and heated 

 milk antisera do not cause this deviation. Antisera obtained by the injection 

 of boiled milk and the constituents of boiled milk showed, in general, a weaker 

 reaction than those obtained by the injection of the raw milk and its con- 

 stituents. 



Of the individual constituents of milk, the milk serum shows specific charac- 

 teristics as does blood serum. The animal specificity of the casein is not so 

 regular. 



It is indicated from the experiments that a specificity of milk may be con- 

 sidered in the .sense of " organ specificity," which is principally attributable 

 to the casein content. 



The fomiation of specific proteoclastic ferments in response to introduc- 

 tion of placenta, Florence Hulton (Jour. Biol. Chem., 25 (1916), No. 2, pp. 

 227-230). — " Placental protein is not digested to any greater degree by the serum 

 of an animal sensitized to placenta than by the normal serum. The digestive 

 power of the serum of an animal sensitized to placenta is not increased for 

 casein, Bence-Jones protein, phaseolin, edestin, soy-bean globulin, or milk 

 albumin. Casein is digested to a marked degree by the normal serum, and in 

 most cases the normal serum possesses the more marked activity. Protamiu is 

 digested to a marked degree in both cases, the injected animal showing in- 

 creased activity. Gliadin is not digested to any great extent by the normal 

 serum, but is by the serum of the injected animal. In general, it may be said 



