208 Kihne and Chittenden— Globulin and Globulose Bodies. 
As we hope to show, however, the results gained in the study of 
the albumose bodies from fibrin are by no means to be considered as 
valueless, but on the other hfand as quite advantageous in the treat- 
ment of the single albumins, particularly as an aid in the separation 
of the individual albumose bodies. Thus in our study of globulin, 
now to be described, we were able to use methods already tested. 
The new method of precipitating albumose bodies by ammo- 
nium sulphate, which has meanwhile been discovered and which is 
certainly particularly advantageous, has not been used in our 
study of the globulose bodies, since these experiments were con- 
cluded before the introduction of that method. According to obser- 
vations made by Dr. Neumeister in the Physiological Institute at 
Heidelberg, ammonium sulphate appears particularly well adapted 
to the purification of deuteroalbumose, since after complete removal 
of protoalbumose by sodium chloride and acid, deuteroalbumose 
alone is precipitated by addition of the ammonium salt. As, how- 
ever, we had accomplished a separation of the different globulose 
bodies in another manner, it seemed unnecessary to use, in addition, 
the new method. 
Globulin. 
From the list of albuminous bodies which occur in sufficient quan- 
tity, and which at the same time admit of isolation without too great 
difficulty we have chosen for our first study, globulin. The substance 
was prepared from the serum of ox blood by the method of Hammar- 
sten, in which repeated quantities of fresh serum were treated with 
an excess of crystallized magnesium sulphate at a temperature of 
30° C. The precipitate so obtained was collected on a filter, washed 
with a saturated solution of the salt, pressed, dissolved in water, and 
reprecipitated a second time by the addition of magnesium sulphate. 
The precipitate was then dissolved in water, a little thymol added, ~ 
and the solution dialyzed in running water in order to remove the 
magnesium salt. The final solution was then concentrated at 40° C,, 
after which the globulin was precipitated with alcohol, washed with 
alcohol and finally extracted with ether. The substance so prepared, 
and which still contained some magnesium sulphate, was employed — 
in the digestion experiments. A portion of the preparation, dried 
at 110° ©. in vacuo, gave by analysis the results contained in 
the following table. The methods of analysis were the same as 
those employed in our previous work.* 
* Compare Zeitschrift fiir Biologie, Band xx, p. 11, and Amer. Chem. Jour., vol 
vi, p. 3. 
