oxiDi'/.iSd i:\/.) ][j:s 71 



lar decrease in eatalase, including primary anemias and the secondary- 

 anemias of typhoid and pneumonia; cardiac disease has no effect if 

 tlie kidneys are normal. Acute peritonitis causes a rise in l)lood 

 eatalase; diabetes, leukemia and jaundice were without effect. In 

 hyperthyreosis the eatalase tends to increase, in hypothyreosis to de- 

 crease; complete removal of the thyroid causes a decrease which disap- 

 pears on feeding thyroid. Intravenous injection of salts, acids and 

 alkalies decreases the catalytic activity of the blood. Normal indi- 

 viduals show considerable variations in the eatalase activity of the 

 blood, but for each individual it is remarkably constant ; age has very 

 little influence. In the tissues post mortem change causes but slight 

 reduction in eatalase. Extirpation of large amounts of kidnc}' or liver 

 tissue has little effect, but removal of the spleen, ovaries or testicles 

 causes a transient decrease in the eatalase of the blood. If the red 

 corpuscles are prevented from laking, the eatalase activity manifested 

 by the blood in vitro is reduced (Strauss) ^~ and iodides increase the 

 eatalase activity of the blood. Catalase and anticatalase have been 

 found in pathological urine, in both acute and chronic nephritis 

 (Primavera).*^ Kahn and Brim ^^'^ also found traces of catalase in 

 normal urine, greatly increased in urine containing blood, bile or ace- 

 tone, normal in cancer, high in diabetic acidosis, Hodgkin's disease, 

 septic infections and typhoid. Grossman ^* found that bacterial poi- 

 sons generally increase the catalase content of the various viscera, and 

 Rosenthal *^ observed a great decrease in the liver and blood of mice 

 receiving intraperitoneal inoculations of cancer. The catalase activity 

 of the non-cancerous organs of cancer patients is not affected, except 

 slightly lowered by cachexia (Col well) ^®; however, the liver tissue 

 between cancer nodules may show less catalase than normal liver. ^*''* 

 True Oxidizing Enzymes. — AVhile it is by no means certain that 

 catalase is active in causing intracellular oxidations, there are other 

 enzymes or enzyme-like substances that come more properly under the 

 head of oxidases or oxidizing enzymes. Battelli and Stern contend 

 that the only real oxidases which have yet been completely established 

 are: 1. Polyphenoloxidases (oxidizing phenols and their amino com- 

 pounds, but not tyrosine) ; 2. Tyrosinase; 3. Alcohol oxidase; 4. Xan- 

 thine oxidase ; 5. Uricase. Chodat and Bach believe that the enzymes 

 which are designated above as polyphenoloxidases have a complex 

 structure, consisting of peroxidase and oxygenase. Mathews **"^ holds 

 that "under the term oxidases there have been confused two classes 



82 Bull. .Johns Hopkins Hosp., 1912 (23), 120. 



83 Riforma Med.. 1906 (12), 1206. 

 83aAmer. .Jour. Obst.. 1915 (71). 39. 

 84Biochem, Zeit.. 1912 (41), ISl. 

 85Deut. med. Woch.. 1912 (38), 2270. 



86 Arch. Middlesex Hosp., 1910 (19), 64. 



86a Blumenthal and Brahn, Zeit. KrebsforBcli., 1910 '8), 436. 



86b Jour. Biol. Chem., 1909 (6), 1. 



