Chittenden and Bolton—Egg-Albumin and Albumoses. 351 
Digestion of albumin B. 
340 grams of the dry albumin, non-coagulated, were soaked in 2 
litres of 0-4 per cent. hydrochloric acid for 24 hours, then warmed up 
to 45° C. and 1 litre of the purified pepsin-hydrochloric acid added, 
also warmed at the same temperature. The mixture was kept at 
45° C. for 16 hours, then neutralized and filtered. The filtrate, con- 
taining the albumose bodies formed from the non-coagulated albu- 
min, was then treated as already described under Albumin A. 
B. Protoalbumose. 
The protoalbumose isolated from this digestion, was purified in 
much the same manner as A protoalbumose, and did not differ from 
it in its reactions, except that with water it did not dissolve to quite 
so clear a solution; in fact its solution in water resembled more 
closely the aqueous solutions of protoalbumose from fibrin. During 
its final purification, it was dialyzed in running water until no chlorine 
reaction could be obtained with silver nitrate. In spite of this fact, 
however, the preparation contained a large percentage of ash, con- 
sisting mainly of calcium sulphate, ferric oxide and a little calcium 
phosphate. 
The accompanying table shows the composition of the substance 
after drying at 106° C., im vacuo, until of constant weight. 
In the purification of this protoalbumese, the substance was repre- 
cipitated three times by saturating the aqueous solution of the pre- 
cipitate with sodium chloride. By this treatment, as already stated, 
there is considerable loss, inasmuch as the precipitation of proto- 
albumose with salt in this manner is never complete, considerable 
remaining each time in the salt-saturated fluid. By adding a very 
little acetic acid, however, the protoalbumose is completely precipi- 
tated from the salt-saturated solution. The filtrates therefore, from 
the second and third precipitations of protoalbumose with salt 
alone were united, and the albumose remaining in them precipitated 
by the addition of a little acetic acid, saturated with sodium chloride. 
Our object was to see whether the protoalbumose which had at one 
time been precipitated by salt alone. and then had finally become 
soluble in the salt-saturated fluid, differed at all in composition or in 
reaction from the protoalbumose still insoluble in the salt solution. 
The albumose separated in this manner was purified by being dis- 
solved in water, the solution made exactly neutral with sodium car- 
bonate and dialyzed for several days. The fluid was then con- 
