A\Tf-K\Z)]n:,<< 65 



normal horse serum is in the pseu(l()<il()l)ulin fraction. Since acids 

 destroy the anti-enzyme property of the serum, it is not effective 

 against pepsin-IICl mixtures. Against trypsin, however, it is very 

 effective. Zniiz ■'- states that normal serum acts more upon entero- 

 kinase than upon try!)sin, and believes tlmt the inliibition depends 

 upon colloids which modify surface tension and adhere to the pro- 

 teins. Red corpuscles and living unicellular organisms, including 

 bacteria, are likewise resistant to trypsin, and normal serum also 

 seems to contain an antirennin."'? Fresh and inactivated serum will 

 prevent pepsin from digesting protein, but this is not due to a true 

 antipepsin, according to Hamburger.^* Oppenheimer and Aron ^^' 

 consider it probable that the resistance of normal serum to trypsin di- 

 gestion depends upon the configuration of the protein molecules, which 

 perhaps, when in fresh, uninjured condition, present no suitable sur- 

 faces for attack by the ferment. 



Jobling '^■'"- and his co-workers have advanced evidence that the nor- 

 mal antiprotease action of serum depends on the lipoids of the serum, 

 which vary in activity directly with the degree of uusaturation ; there- 

 fore they were able to decrease the antiferment action of serum by 

 extracting the lipoids with fat solvents (and to restore the activity 

 by replacing the lipoids), or by saturating the double bonds of the 

 fatty acids with halogens, or by modifying the degree of dispersion 

 of the lipoids. Soaps of saturated fatty acids do not inhibit serum 

 protease. 



Opie ■''' has found that the serum of inflammatory exudates con- 

 tains an anti-enzymatic substance, destroyed at 75°, and by acids; 

 it is not present in normal cerebrospinal fluid, but appears here as 

 in other serous cavities during inflammation (Dochez).'^" Antitrypsin 

 has also been found in pathological urines (v. Sclioenborn).^^ 



The power of the blood semm to inhibit the activity of trypsin and 

 leucocytie protease has been found to vary greatly in disease, and, as 

 having diagnostic possibilities, this property has been considerably 

 investigated.^^ It is especially increased in conditions associated with 

 cell destruction, such as pneumonia and cancer, which suggests that 



52 JTem. Acad. roy. med. Bclgiqiie, 1909 (20). fase. 5. 



53Czapek (Ber. Deut. botan. Gesell., 1903 (21), 229) states lliat anti-oxidases 

 occur normally in certain plants, strongly specific aprainst tlie oxidase of the 

 same plant species. 



54 .Jour. Exper. 'Sled., 1911 (14), .5.35; Arcli. Tnt. ^led., 1915 (16), .350. There 

 seems to be no relation between the antipeptic and antitrvptic powers of sera 

 (Rubinstein, Ann. Inst. Pasteur., 1913 f27). 1074). 



5- Hofmeister's Beitriige, 1903 (4), 279. 



55a Series of articles in Jour. Exper. ^led. : also review in .Tour. T.al). and Clin. 

 Med.. 1915 (1), 172. See also Zeit. Tmmunitiit., 1914 (23), 71. 



50 Jour. Exp. Med.. 1905 (7). 31fi. 



57, Jour. Exper. Med., 1909 (11), 718. 



5sZeit. f. Biol., 1910 (53), 386. 



59 For literature and review see Wiens, Erjiebnisse Phvsiol.. 1911 (15). 1; 

 Weil, Arch. Int. Med., 1910 (5), 109; Meyer, Folia Serologica, 1911 (7), 471. 



5 



