Kiihne and Chittenden— Globulin and Globulose Bodies. 213 
the turbidity, however, disappearing completely as the solution be- 
came cool, (the opposite of the albumose reaction : compare Zeitschrift 
fiir Biologie, Band xx, p. 45), We think it may be assumed that this 
single deviation from the reactions of fibrin-protoalbumose is not 
due to the presence of impurities (heteroglobulose, etc.), because no 
heteroglobulose whatever separated from a portion of the sample, 
even after dialyzing a week longer. If the solution was made even 
very slightly acid or alkaline, the turbidity did not then occur on 
heating. Further, the small content of ash (0:4 per cent.), which con- 
sisted only of calcium sulphate with a trace of ferric oxide, testifies 
to the purity of the preparation and the completeness of the dialysis. 
The preparation was analyzed with the results shown in the accom- 
panying table. 
Deuteroglobulose. 
This body is about as difficult to purify from the preceding one as 
deuteroalbumose from protoalbumose. We succeeded, however, in 
separating it by rejecting the first portions of the precipitate pro- 
duced by acetic acid and sodium chloride and using only the last 
portions precipitated; or after the acetic*acid failed to give 
any further precipitate, by using the small precipitate produced 
by the moderate addition of alcohol. This last precipitate naturally 
enclosed considerable sodium chloride, but the deuteroglobulose 
was obtained perfectly pure after removing the salt by dialysis, 
since the globulose solution, even when noticeably acid, gave 
no turbidity whatever on the addition of salt in substance. The 
quantity, however, was unfortunately too small for analysis. It suf- 
ficed only for determining the reactions, which agreed with those of 
the substance obtained by the later precipitation with acetic acid 
except in one particular, viz: that the latter preparation in a neutral 
_ or slightly alkaline solution showed an extremely slight turbidity on 
the addition of crystals of sodium chloride. All other reactions were 
identical and corresponded so completely with those of deutero- 
albumose that it is only necessary to call attention to the latter (see 
Zeitschrift fiir Biologie, Band xx, pp. 26-28, or Amer. Chem. Jour., 
vol. vi, pp. 46-47) and to especially mention the non-precipitation of 
deuteroglobulose in a solution free from salt, by nitric acid in any 
quantity and at any temperature. 
Since no heteroglobulose whatever eeaicd from the solution of 
the last acetic acid precipitate during dialysis, even with repeated 
change of reaction, the substance was therefore prepared for analysis, 
