1918] 
BONNS—ETHERIZATION AND ENZYME ACTIVITY 279 
largely accounted for by the greater normal hydrolysis of 
the easein. In neutral solution the dispersion from etherized 
tissues again shows a greater activity than that from the un- 
etherized corms. In alkaline solution A 1 is markedly less 
than В 1. Whether this is due to the condition of the medium 
with respect to the enzyme cannot be determined, unfortu- 
nately, since the flask of enzyme control of the second half of 
this series, D 1, was lost during incubation. It is conceivable 
that such a great difference might be the result of an error 
in adding the enzyme dispersion twice to the same flask in 
preparing the series, although care was taken in this respect. 
In the peptone substrates, both alkaline and neutral, a retar- 
dation or inhibition of the activity of the enzyme from ether- 
ized tissues may be noted. This holds for both halves of the 
series. As a whole, the amount of hydrolysis in the peptone 
series bears a close relation to that obtained with easein, and 
is again much greater than that of albumin. In view of the 
consistent relation of the results with albumin and peptone, 
in the two halves of a series as well as in acid and alkaline 
media, we are inclined to ascribe the increased value of B 1 
over A 1 in the casein alkaline series to an error of manipu- 
lation rather than to any effect upon enzyme action. 
In a consideration of the carbohydrate experiments atten- 
tion was ealled to the probable effect on hydrolysis of the 
previously autoclaved dispersions. This appears in several 
instances in the table above, but the effect is by no means 
uniform. In three cases (albumin alkaline D 2, and casein 
neutral B2 and D2) it relates to the dispersion from un- 
etherized tissues, and in three others (casein neutral C 2, and 
peptone neutral C 2 and alkaline C 2), to the controls. No ex- 
planation seems sufficient to account for an increase in value 
obtained from these flasks over those with the corresponding 
letters, unless such increase is due to the products resulting 
from the disintegration of the previously autoclaved disper- 
sion. In support of this probability is the value for casein 
neutral C 2, which, after the second autoclaving, was by mis- 
take subjected to a third autoclaving by another worker in 
the laboratory. It would appear that the increased number 
