326 BOTANICAL GAZETTE [MAY 
no peptonizing enzyme, but does have an enzyme which, like erepsin 
of the animal body, attacks albumoses and peptones. In cases 
where all the trials were made with the addition of Witte peptone, 
it is impossible to say whether there is an enzyme present of the 
trypsin type (tryptase), the erepsin type (ereptase), or both. In 
cases where a positive result was obtained both with or without 
the addition of Witte peptone, a tryptase is present if, as is probable, 
the tissue contains no marked quantity of albumoses or peptones; 
an ereptase may also be present and in the table its presence is indi- 
cated as questionable. When no tryptophan reaction is given on 
autolysis, except after the addition of a proteose, I have assumed 
that no tryptase was present, an assumption which, as pointed out 
above, is not entirely justified because certain proteids give no reaction 
for the tryptophan radical (see table). 
This table records but three failures to obtain evidence of a pro- 
tease, the pulp of the apple, the juice of the orange, and the sap 
of the bleeding birch tree (Betula alba), which last is not a cell extract. 
The two failures, the apple and the orange juice, are scarcely suffi 
cient to prevent the acceptance of these results as evidence of the 
‘universal occurrence of proteases in living plant tissues. 
No mention has been made of the proteolytic enzymes of the 
insectivorous plants and the bacteria and lower fungi. Some of 
the latter are doubtless endo-enzymes and belong to the group which 
I have termed metabolic enzymes. The others are apparently 
secretions designed to render food materials available and should 
be classed with the digestive enzymes. 
The results of Vines tend to show that there are enzymes of the 
erepsin type widely distributed in plants, yet the evidence is not 
wholly conclusive and he has made no attempt to isolate such enzymes 
DELEZENNE and Mouton’? made extracts from several fleshy fungi, 
Amanita muscaria, Amanita citrina, Hypholoma fasciculare, and 
Psalliota (Agaricus) campestris, which were judged to contain an 
ereptase since they digested proteoses but not fibrin. VINES finds, 
however, that Agaricus campestris, which DELEZENNE and MOUTON 
found to yield an especially active ereptase, is capable of autolysis 
and will digest fibrin if the fibrin is not boiled. The unboiled fibrin 
76 DELEZENNE and Mouton, Compt. Rend., April 9, 1903- 
