OXIDIZING ENZYMES 65 



corpuscles. Catalase is abundant in the tissues of lower animal forms, e. g., 

 Ascaris.^" Substances decomposinp; HoOj have been found also in bacterial cul- 

 tures, first by Gottstein, and later in the cell juices expressed from tubercle bacilli 

 by Hahn. Locwenstein" found an enzyme aRreeinp; with catalase in filtered bouillon 

 cultures of diphtheria bacilli and staphylococci, l)ut not frorn tetanus, typhoid, 

 and colon bacilli or cholera vibrios; the catalase is quite distinct from the toxin. 

 He also found that the addition of H2O2 to a diphtheria toxin-antitoxin mixture 

 destroyed the toxin, leaving the antitoxin free. A similar destruction of tetanus 

 toxin l)y peroxides, first demonstrated by Sieber, can occur without the catalase. 



Winternitz^- and his associates have made extensive studies of the catalase 

 activity of the blood and tissues in disease. They found that all tissues have re- 

 duced catalase activity in chronic nephritis, in proportion to the severity of the 

 condition, and experimental nephritis in animals has the same effect; the blood 

 shows great reduction in catalase in vu-emia, and a less reduction with less severe 

 nephritic manifestations. Eclampsia shows little or much reduction of catalase 

 in the blood in proportion to the amount of renal involvement; normal pregnancy 

 and labor have no elTect. Anemia is associated with irregular decrease in catalase, 

 including primary anemias and the secondary anemias of typhoid and pneumonia; 

 cardiac disease has no effect if the kidneys are normal. Acute peritonitis causes a 

 rise in blood catalase; diabetes, leukemia and jaundice were w-ithout effect. In 

 hyperthj-reosis the catalase tends to increase, in hypothyreosis to decrease; com- 

 plete removal of the thyroid causes a decrease which disappears on feeding thy- 

 roid. Intravenous injection of salts, acids and alkalies decreases the catalytic 

 activity of the blood. In shock, blood catalase is decreased." Normal indi- 

 viduals show considerable variations in the catalase 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 catalase. Extirpation of 

 large amounts of kidney or liver tissue has little effect, but removal of the spleen, 

 ovaries or testicles causes a transient decrease in the catalase of the blood. In 

 diabetes and starvation, tissue catalase is said to be decreased.'^ If the red cor- 

 puscles are prevented from laking, the catalase activity manifested by the blood in 

 vitro is reduced (Strauss)'* and iodides increase the catalase 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 cata- 

 lase in normal urine, greatly increased in urine containing blood, bile or acetone, 

 normal in cancer, high in diabetic acidosis, Hodgkin's disease, septic infections and 

 typhoid. Grossman'* foimd that bacterial poisons 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 (Colwell) ;'° however, the liver tissue between 

 cancer nodules may show less catalase than normal liver. •^' In phosphorus poi- 

 soning the catalase content of the liver, heart and blood is decreased (Burge).'-' 



But it is to be borne in mind that the questionable accuracy of our existing 

 methods of determining quantitatively the amount or activity of catalase in tis- 

 sues makes the foregoing statements of uncertain value. 



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

 catalase is active in causing intracellular oxidations, there are other 



'0 Magath, Jour. Biol. Chem. 1918 (33), 395. 



" Wien. klin. Woch., 1903 (16), 1393. 



12 Review in Arch. Int. Med., 1911 (7), 624. 



»3 Burge and Neill, .\mer. Jour. Physiol., 1918 (45), 286. 



1* Burge, Science, 1918 (47), 347. 



'6 Bull. Johns Hopkins Hosp., 1912 (23), 120. 



'6 Riforma Med., 1906 (12), 1266. 



" Amer. Jour. Obst., 1915 (71), 39. 



18 Biochem. Zeit., 1912 (41), 181. 



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



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



21 Blumenthal and Brahn, Zeit. Krebsforsch., 1910 (8), 436. 

 " Amer. Jour. Phvsiol., 1917 (43), 545. 



