THE RELATION BETWEEN OXIDASE AND CATALASE 
IN PLANT TISSUES 
G. B. REED 
(WITH ONE FIGURE) _ 
In a previous paper" the writer has pointed out that although 
substances which act as oxidases or peroxidases usually decompose 
hydrogen peroxide, and although many authors think that there is 
a causal connection between the two processes, yet in the case of 
colloidal platinum they are quite independent. The question then 
arises, to what extent does this apply to the living cell? This is 
of particular interest in view of the fact that some investigators 
suppose that oxidase action depends in some way upon the activity 
of a catalase. 
A few instances are on record in which, by some special treat- 
ment, plant oxidases have been prepared so as to give no catalase 
action. LirBERMANN? found that by shaking an extract of malt 
with mercuric oxide and magnesia, or by heating the extract to 
80° C., its catalase activity was destroyed but it still exhibited some 
peroxidase action. Lorw’ reports that after treating an aqueous 
extract of fresh tobacco with one-fifth its volume of absolute alco- 
hol it had no action on hydrogen peroxide, but still activated 
directly the oxidation of gum guaiac. Finally, Kasansxr has 
shown that the catalase action of certain plant and animal extracts 
may be destroyed by the addition of strong solutions of pyrogallol 
or sugar, without completely inhibiting their peroxidase action. 
More conclusive evidence that peroxidase action is independent 
of any ability to decompose hydrogen peroxide was obtained by 
the writer from a study of pineapple extracts. Pineapple juice 
always contains very active peroxidases; catalase reactions were 
* REED, G. B., Bor. Gaz. 62:233-238. 1916. 
* LIEBERMANN, P., and L., Pfliiger’s Archiv. 108:489-495. 1905. 
3 Loew, O., Report no. 68. U.S. Dept. Agric., p. 47. 1901. 
* KasanskI, Biochem. Zeit. 39:64—-72. 1911. 
409] [Botanical Gazette, vol. 62 
