1916] 
ZELLER—PHYSIOLOGY OF LENZITES SAEPIARIA 499 
Where casein, legumin, and albumin were used as substrates 
there was no indication of digestion in either the mycelial or 
sporophoral dispersion. In no case was there positive proof 
of peptonization. Peptone, however, was peptolyzed in 
neutral, alkaline, and acid solutions. If any distinction can 
be made there was stronger indication of tryptophan in the 
acid and alkaline solutions than in neutral Quantitative de- 
terminations were not made. 
Action on fibrin.—The digestion of fibrin was determined 
by using the method described by Reed (713). Fibrin was 
stained in 1 per cent Congo red, and the color fixed by im- 
mersion in hot water. When such fibrin is acted on by trypsin 
the red color is liberated into the solution. With this colored 
fibrin in water as a substrate, negative results were obtained 
with the mycelial and sporophoral dispersions. Toluol was 
used as an antiseptic. Another series of tubes was set up, 
using 6 grams of mycelial meal in 10 cc. of water and the 
colored fibrin as a substrate. In this case potassium cyanide 
was used as an antiseptic, and the results were positive. The 
color value in this case was difficult to judge, however, on 
account of the brown color imparted to the solution by the 
sawdust meal, but the tryptophan test confirmed the color 
liberation. 
The question arose whether potassium cyanide is a better 
antiseptic than toluol, use of the first-mentioned having been 
recommended by Vines in certain cases. Later experiments 
were conducted, using the pure mycelium grown on carrot 
juice as a source of enzymes, while potassium cyanide, toluol, 
and thymol-chloroform were used as antiseptics. In this 
series pure fibrin in water was the substrate. In all of these 
except two, after digestion of two weeks, the tryptophan test 
was obtained, the exceptions being those of the autoclaved 
controls and water controls. The test was slightly more dis- 
tinct where potassium cyanide was used as an antiseptic. 
The results are sufficient to demonstrate the presence of 
both erepsin and trypsin in the mycelium, and at least erepsin 
in the sporophores of L. saepiaria. 
