THE SEPARATION OF OXIDASE REACTIONS FROM 
THE CATALASE REACTION 
G.-B:. REED 
(WITH THREE FIGURES) 
It is an interesting fact that, with one or two exceptions, the 
oxidases of plant and animal tissue, even when purified by the best 
existing methods, still give the catalase reaction, that is, decompose 
hydrogen peroxide with the evolution of oxygen in ‘its molecular 
or relatively inactive form. The relation of this catalase action to 
the physiological activity of the organism is not understood, 
: although several explanations have been advanced. 
LoEw' was the first to isolate a body capable of decomposing 
hydrogen peroxide but possessing no other enzyme properties. 
This body he called catalase. Many investigations since this time 
have proved the correctness of Lorw’s results. SENTER? prepared 
from blood a catalase free from haemoglobin or oxidases. LIEBER- 
MANN’ has shown that aqueous extracts of the mesenteric fat of 
hogs and rabbits decompose hydrogen peroxide without showing 
any oxidase reactions. Catalase in every way similar to that 
isolated by Lorw has also been prepared by WENDER' from yeast, 
and by Pazz1-Escors from various higher plants. 
As a result of his observations, Lorw (loc. cit.) reached the 
conclusion that catalase is universally distributed, occurring not 
only in every organism but in every living cell. He assumed, 
therefore, that it must have some definite function. Since hydrogen 
peroxide results from the oxidation of many readily oxidizable 
substances, he regarded it as at least conceivable that this com- 
pound may be produced in the living cell as a result of respiratory 
processes. The accumulation of such a substance would doubtless 
* Loew, O., Report no. 68. U.S. Dept. Agric. p. 47. 190r. 
? SENTER, G., Zeit. Physikal. Chem. 44:257-263. 1903; 51:673-705. 1905. 
3’ LreBERMAnN, L., Pfliiger’s Archiv. 104: 119-233. 1904. 
* WENDER, Chem. Zeit. 28: 300~301, 322-323. 1904. 
’ Pazzt-Escot, Bull. Soc. Chem. Par. 27: 280-288. 1902: 
303] [Botanical Gazette, vol. 62 
